Source 1primary paper2014生物物理
Toolkit/AsLOV2
AsLOV2
Also known as: asLOV2, AsLOV2, AsLOV2-based optogenetic tools, AsLOV2 domain, AsLOV2 photoreceptor, Avena sativa LOV2, Avena sativa phototropin 1 LOV2, Avena sativa phototropin 1 LOV2 domain, Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, isolated LOV domain AsLOV2, Light-Oxygen-Voltage 2 (LOV2) domain of Avena sativa phototropin 1, light-oxygen-voltage domain 2 of Avena sativa, light-oxygen-voltage-sensing domain 2 of Avena sativa, light-oxygen voltage sensitive domain from Avena sativa, LOV2, LOV2 domain, LOV2 domain from Avena sativa phototropin 1, LOV2 domain of Avena sativa phototropin 1, LOV2 domain of Avena sativa phototropin-1, LOV2 domain of the flavin binding phototropin Avena sativa, Q513A variant of AsLOV2, second LOV domain of Avena sativa phototropin 1, the second LOV domain derived from Avena sativa phototropin 1
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
AsLOV2 is the light-oxygen-voltage 2 photosensory domain from Avena sativa phototropin 1 used as a blue-light-responsive actuator in engineered fusion proteins. Blue-light activation drives allosteric conformational extension involving sequential unfolding of the N-terminal A'α helix and the C-terminal Jα helix, enabling conformational uncaging and related optogenetic control.
Usefulness & Problems
Why this is useful
AsLOV2 is useful as a genetically encoded light-responsive domain that converts blue-light input into a protein conformational change that can be coupled to engineered outputs. The cited literature also supports its use in applied designs such as an AsLOV2-based degron for BIC-light-activated gene expression in plants and in photoswitchable peptide engineering via circular permutation.
Source:
methionine introduction invariably impairs photoactivation efficiency and thus renders the resultant AsLOV2 variants less light-sensitive
Source:
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
Source:
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
Source:
We present time‐resolved Gd−Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter‐residue distances during a protein's mechanical cycle in the solution state.
Problem solved
AsLOV2 helps solve the problem of externally controlling protein activity with light by providing a compact photosensory domain whose activation propagates long-range structural changes. The hydraulic activation study further frames this as a route to engineering externally controllable protein actuators.
Source:
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
Source:
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
Source:
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Source:
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Problem links
Need better screening or enrichment leverage
DerivedAsLOV2 is the light-oxygen-voltage 2 photosensory domain from Avena sativa phototropin 1 that serves as a blue-light-responsive actuator in engineered fusion proteins. Upon activation, it undergoes allosteric conformational extension with sequential unfolding of the N-terminal A'α helix and the C-terminal Jα helix, enabling conformational uncaging and related optogenetic outputs.
Need conditional control of signaling activity
DerivedAsLOV2 is the light-oxygen-voltage 2 photosensory domain from Avena sativa phototropin 1 that serves as a blue-light-responsive actuator in engineered fusion proteins. Upon activation, it undergoes allosteric conformational extension with sequential unfolding of the N-terminal A'α helix and the C-terminal Jα helix, enabling conformational uncaging and related optogenetic outputs.
Need conditional recombination or state switching
DerivedAsLOV2 is the light-oxygen-voltage 2 photosensory domain from Avena sativa phototropin 1 that serves as a blue-light-responsive actuator in engineered fusion proteins. Upon activation, it undergoes allosteric conformational extension with sequential unfolding of the N-terminal A'α helix and the C-terminal Jα helix, enabling conformational uncaging and related optogenetic outputs.
Need inducible protein relocalization or recruitment
DerivedAsLOV2 is the light-oxygen-voltage 2 photosensory domain from Avena sativa phototropin 1 that serves as a blue-light-responsive actuator in engineered fusion proteins. Upon activation, it undergoes allosteric conformational extension with sequential unfolding of the N-terminal A'α helix and the C-terminal Jα helix, enabling conformational uncaging and related optogenetic outputs.
Need precise spatiotemporal control with light input
DerivedAsLOV2 is the light-oxygen-voltage 2 photosensory domain from Avena sativa phototropin 1 that serves as a blue-light-responsive actuator in engineered fusion proteins. Upon activation, it undergoes allosteric conformational extension with sequential unfolding of the N-terminal A'α helix and the C-terminal Jα helix, enabling conformational uncaging and related optogenetic outputs.
Workflow Fit
Likely fit
- •fast-no-cloning-screen: useful when evaluating a known fusion design or a small candidate set
- •standard-construct-loop: useful when tuning architecture, linker choice, localization, or host-specific performance
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational uncagingconformational uncagingconformational uncagingConformational Uncaginghelix unfoldinghelix unfoldinghelix unfoldinghydration-shell water expulsionhydration-shell water expulsionhydration-shell water expulsionhydraulic activationhydraulic activationhydraulic activationlight-induced allosteric switchinglight-induced allosteric switchinglight-induced allosteric switchingTechniques
Computational DesignDirected EvolutionFunctional AssaySelection / EnrichmentStructural CharacterizationTarget processes
localizationrecombinationselectionsignalingInput: Light
Output: Conformational Change
Implementation Constraints
cofactor dependency: cofactor requirement unknowncontrol mode: conformational photoswitchingencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementmodule family: LOV-domain systemoperating role: actuatoroperating role: regulatoroperating role: sensorswitch architecture: single chainswitch architecture: splitswitch architecture: uncaging
AsLOV2 is a domain from Avena sativa phototropin 1 and is activated by blue light; the cited physical chemistry literature also implicates FMN ground-state electronic structure and a conserved cysteine in LOV2 photochemistry. Practical engineering approaches supported by the sources include domain fusion, circular permutation, site-directed mutagenesis, and screening for fast- and slow-cycling variants. One cited study reports that imidazole can efficiently enhance dark recovery of AsLOV2, indicating that recovery kinetics can be chemically modulated under some conditions.
The supplied evidence is strong for mechanism but limited for quantitative performance metrics such as dynamic range, recovery time in specific constructs, photostability, or context dependence across host systems. Application evidence is present but sparse in the provided claims, so breadth of validated outputs and independent benchmarking against alternative optogenetic actuators cannot be established here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freemechanistic demo
Inferred from claim c3 during normalization. Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s. Derived from claim c3. Quoted text: Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
relaxation time constant60 sseparation time1 s(<)
successCell-freeapplication demo
Inferred from claim c4 during normalization. The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore. Derived from claim c4. Section: abstract. Quoted text: TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
successCell-freeapplication demo
Inferred from claim c4 during normalization. The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore. Derived from claim c4. Section: abstract. Quoted text: TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
successCell-freeapplication demo
Inferred from claim c4 during normalization. The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore. Derived from claim c4. Section: abstract. Quoted text: TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
successCell-freeapplication demo
Inferred from claim c4 during normalization. The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore. Derived from claim c4. Section: abstract. Quoted text: TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
successCell-freeapplication demo
Inferred from claim c4 during normalization. The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore. Derived from claim c4. Section: abstract. Quoted text: TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
successCell-freeapplication demo
Inferred from claim c4 during normalization. The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore. Derived from claim c4. Section: abstract. Quoted text: TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
Supporting Sources
Source 2primary paper2024Journal of Computational Chemistry
Source 3primary paper2007Biochemistry
Source 4primary paper2020
Source 5primary paper2021eLife
Source 6primary paper2021
Source 7primary paper2021Chemical Communications
Source 8primary paper2016Physical Chemistry Chemical Physics
Source 9primary paper2024Methods in molecular biology
Source 10primary paper2023
Source 11primary paper2021Journal of the American Chemical Society
Source 12primary paper2013PLoS ONE
Source 13review2015Photochemical & Photobiological Sciences
Source 14primary paper2008Physical Chemistry Chemical Physics
Source 15primary paper2022ACS Synthetic Biology
Source 16primary paper2021Physical Chemistry Chemical Physics
Source 17primary paper2015Proceedings of the National Academy of Sciences
Source 18primary paper2012Journal of Molecular Biology
Source 19primary paper2023Angewandte Chemie International Edition
Source 20primary paper2022
Source 21primary paper2017Biochemistry
Source 22primary paper2025
Source 23primary paper2025
Source 24primary paper2024RSC Chemical Biology
Source 25primary paper2021Computational and Structural Biotechnology Journal
Source 26primary paper2020
Source 27primary paper2020ACS Chemical Biology
Source 28primary paper2019ACS Omega
Source 29primary paper2017The Journal of Physical Chemistry B
Source 30primary paper2015ACS Synthetic Biology
Source 31primary paper2014PLoS ONE
Source 32primary paper2011Photochemistry and Photobiology
Source 33primary paper2011Biochemistry
Source 34primary paper2008Biochemistry
Ranked Claims
The reported hydraulic activation concept offers a new concept for engineering externally controllable protein actuators.
offers a new concept for engineering externally controllable protein actuators
AsLOV2 activation can be initiated by blue light or high pressure and is followed by selective and concerted expulsion of low-entropy, tetrahedrally coordinated wrap water from the protein hydration shell.
we find AsLOV2 activation can be initiated by blue light or high pressure, followed by selective and concerted expulsion of low-entropy, tetrahedrally coordinated "wrap" water from the protein hydration shell
Blue light activation of AsLOV2 gives rise to concerted water movement that induces protein conformational extensions.
This study tests the hypothesis that blue light activation of the LOV2 (light, oxygen, voltage sensitive) domain of Avena sativa phototropin 1 (AsLOV2), gives rise to concerted water movement that induces protein conformational extensions.
Interfacial water reshapes the protein free energy landscape during AsLOV2 activation and acts as an active hydraulic fluid driving long-range conformational changes upon light activation.
These findings suggest that interfacial water serves as constituents to reshape the protein's free energy landscape during activation. Our study highlights hydration water as an active hydraulic fluid that can drive long-range conformational changes underlying protein mechanics upon light activation
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
Effects of individual methionine substitutions on signaling-state stability and downstream allosteric responses do not show a clear-cut correlation with redox properties.
Although individual methionine substitutions also affect the stability of the signaling state and downstream allosteric responses, no clear-cut correlation with the redox properties emerges.
Targeted modification of the chromophore environment may mitigate intracellular partial reduction effects and enable design of LOV receptors with stratified redox sensitivities.
The targeted modification of the chromophore environment, as presently demonstrated, may mitigate this effect and enables the design of LOV receptors with stratified redox sensitivities.
Methionine substitutions near the flavin increase the reduction midpoint potential of AsLOV2 by up to 40 mV.
Replacements of residues at different sites near the flavin by methionine consistently increase E0 from its value of around -280 mV by up to 40 mV.
reduction midpoint potential shift 40 mV
Methionine introduction impairs photoactivation efficiency and makes AsLOV2 variants less light-sensitive.
methionine introduction invariably impairs photoactivation efficiency and thus renders the resultant AsLOV2 variants less light-sensitive
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
AsLOV2 has a reduction midpoint potential near -280 mV.
With a reduction midpoint potential near -280 mV, AsLOV2
reduction midpoint potential -280 mV
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in the solution state.
We present time‐resolved Gd−Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter‐residue distances during a protein's mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in the solution state.
We present time‐resolved Gd−Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter‐residue distances during a protein's mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in the solution state.
We present time‐resolved Gd−Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter‐residue distances during a protein's mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in the solution state.
We present time‐resolved Gd−Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter‐residue distances during a protein's mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in the solution state.
We present time‐resolved Gd−Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter‐residue distances during a protein's mechanical cycle in the solution state.
frequency 240 GHz
TiGGER is a 240 GHz time-resolved Gd-Gd electron paramagnetic resonance method for tracking inter-residue distances during a protein mechanical cycle in solution.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein's mechanical cycle in the solution state.
Section: abstract
frequency 240 GHz
TiGGER is a 240 GHz time-resolved Gd-Gd electron paramagnetic resonance method for tracking inter-residue distances during a protein mechanical cycle in solution.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein's mechanical cycle in the solution state.
Section: abstract
frequency 240 GHz
TiGGER is a 240 GHz time-resolved Gd-Gd electron paramagnetic resonance method for tracking inter-residue distances during a protein mechanical cycle in solution.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein's mechanical cycle in the solution state.
Section: abstract
frequency 240 GHz
TiGGER is a 240 GHz time-resolved Gd-Gd electron paramagnetic resonance method for tracking inter-residue distances during a protein mechanical cycle in solution.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein's mechanical cycle in the solution state.
Section: abstract
frequency 240 GHz
TiGGER is a 240 GHz time-resolved Gd-Gd electron paramagnetic resonance method for tracking inter-residue distances during a protein mechanical cycle in solution.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein's mechanical cycle in the solution state.
Section: abstract
frequency 240 GHz
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
In AsLOV2, the C-terminal Jα-helix unfolds upon exposure to blue light.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Initiation of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 Jα-helix unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural deviations in N482 could enhance AsLOV2 unfolding rates rather than serving an integral role in unfolding.
the structural deviations in N482, rather than its integral role in unfolding, could enhance the unfolding rates
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 activates AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
Structural reorientation of Q513 enables AsLOV2 to cross the hydrophobic barrier and enter the post-initiation phase of Jα-helix unfolding.
the structural reorientation of Q513 activates the protein to cross the hydrophobic barrier and enter the post initiation phase
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The initiation phase of AsLOV2 Jα-helix unfolding occurs due to collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade.
the initiation phase occurs due to the collapse of the interaction cascade FMN-Q513-N492-L480-W491-Q479-V520-A524
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase in AsLOV2 Jα-helix unfolding is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The onset of the post-initiation phase is marked by breaking hydrophobic interactions between the Jα-helix and the Iβ-sheet.
the onset of the post initiation phase is marked by breaking of the hydrophobic interactions between the Jα-helix and the Iβ-sheet
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
number of unfolding steps 7
The stepwise unfolding of the AsLOV2 Jα-helix was resolved into seven structurally distinguishable steps distributed over initiation and post-initiation phases.
The unfolding was resolved into seven steps represented by the structurally distinguishable states distributed over the initiation and the post initiation phases.
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM analysis of wild-type and Q513 mutant AsLOV2 provides a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
relaxation time constant 60 sseparation time 1 s
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
MSM studies on wild-type and Q513 mutant AsLOV2 provide a spatio-temporal roadmap of possible structural transition pathways between dark and light states.
the MSM studies on the wild type and the Q513 mutant, provide the spatio-temporal roadmap that layout the possible pathways of structural transition between the dark and the light states of the protein
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Section: abstract
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Section: abstract
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Section: abstract
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Section: abstract
relaxation time constant 60 sseparation time 1 s
Upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Using TiGGER, we determined that upon light activation, the C-terminus and N-terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Section: abstract
relaxation time constant 60 sseparation time 1 s
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
Section: abstract
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
Section: abstract
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
Section: abstract
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
Section: abstract
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
The Q513A variant of AsLOV2 shows slowed light-activated long-range mechanical motion, correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Section: abstract
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
AsLOV2 was inserted into selected sites of isocitrate dehydrogenase to construct photoswitchable IDH-AsLOV2 proteins.
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
Engineered IDH-AsLOV2 proteins were used to regulate TCA-cycle metabolic flux in Escherichia coli to improve itaconic acid production.
These engineered light-sensitive proteins were used to regulate the metabolic flux of the tricarboxylic acid (TCA) cycle in <i>Escherichia coli</i> to improve ITA production.
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in solution state.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein’s mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in solution state.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein’s mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in solution state.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein’s mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in solution state.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein’s mechanical cycle in the solution state.
frequency 240 GHz
TiGGER at 240 GHz can track inter-residue distances during a protein mechanical cycle in solution state.
We present time-resolved Gd-Gd electron paramagnetic resonance (TiGGER) at 240 GHz for tracking inter-residue distances during a protein’s mechanical cycle in the solution state.
frequency 240 GHz
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
TiGGER has the potential to complement existing methods for studying triggered functional dynamics in proteins.
TiGGER has the potential to valuably complement existing methods for the study of triggered functional dynamics in proteins.
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The ITA titer was enhanced to 3.30 g/L for strain ITAΔ43 and this strain showed superior photoswitchable potency for ITA production compared with strains that completely deleted icd.
The ITA titer was significantly enhanced to 3.30 g/L for strain ITAΔ43, which displayed superior photoswitchable potency for ITA production compared with the strains that completely deleted the <i>icd</i> gene.
ITA titer 3.3 g/L
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes of blue-light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light without the need of additional chemicals.
activation time within minutes
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
In yeast, LiCre enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
Circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
We demonstrate that the circularly permuted AsLOV2 can be used on its own or together with the original AsLOV2 for enhanced caging.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
The authors demonstrated spatial light control using BLISS by photopatterning two fluorescent proteins.
We demonstrated the spatial aspect of this light control mechanism through photopatterning of two fluorescent proteins.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light, and human cells.
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
LiCre was efficient in yeast and allowed light-controlled production of β-carotene.
LiCre was efficient both in yeast, where it allowed us to control the production of β-carotene with light
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light and lower residual activity in the dark.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre showed faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
QM calculations were used to predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.
QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
The BLISS reaction could be instantaneously quenched by removing light.
Further, the reaction could be instantaneously quenched by removing light.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
AsLOV2 was re-engineered using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
We re-engineered a commonly-used light-sensing protein, AsLOV2, using a circular permutation strategy to allow photoswitchable control of the C-terminus of a peptide.
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Insertion of SpyTag into different locations of the AsLOV2 Jα-helix created a blue-light-inducible SpyTag system called BLISS.
By inserting SpyTag into the different locations of the Jα-helix, we created a blue light inducible SpyTag system (BLISS).
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
Circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In summary, circularly permuted AsLOV2 could expand the engineering capabilities of optogenetic tools.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
In BLISS, SpyTag is blocked from reacting with SpyCatcher in the dark, and blue-light irradiation exposes SpyTag through AsLOV2 Jα-helix undocking.
In this design, the SpyTag is blocked from reacting with the SpyCatcher in the dark, but upon irradiation with blue light, the Jα-helix of the AsLOV2 undocks to expose the SpyTag.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Calculated energies and rotational barriers for glutamine rotamers and tautomers allowed the authors to postulate the most energetically favoured glutamine orientation for each of EL222, AsLOV2, and RsLOV along the assumed reaction path.
Energies and rotational barriers were calculated for possible rotamers and tautomers of the critical glutamine side chain, which allowed us to postulate the most energetically favoured glutamine orientation for each LOV domain along the assumed reaction path.
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Energetic and spectroscopic analyses converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and, more strongly, for AsLOV2, whereas RsLOV retains the initial glutamine configuration.
both the energetic and spectroscopic approaches converge in suggesting a facile glutamine flip at the adduct intermediate for EL222 and more so for AsLOV2, while for RsLOV the glutamine keeps its initial configuration
Beta sheets have a significant role in the overall allosteric process of AsLOV2.
Moreover, the community analysis highlighted the significant role of the β sheets in the overall protein allosteric process.
Maintaining the N-terminal hydrogen bond network is essential for the transition between the light and dark states of AsLOV2.
Maintaining the N-terminal hydrogen bond network was found to be essential for the transition between the two states.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single-chain flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
The authors found three BLISS variants with dynamic ranges greater than 15 and activity in different concentration ranges.
We found three variants with dynamic ranges over 15, which were active within different concentration ranges.
dynamic range 15
Thr407 and Arg410 are key residues involved in the functional conformational switch and affect overall AsLOV2 protein dynamics.
Via in-depth hydrogen bonding and contact analysis we were able to identify key residues (Thr407 and Arg410) involved in the functional conformational switch and their impact on the overall protein dynamics.
AsLOV2 has a monomeric structure in both light and dark states and a relatively short transition time between the two states.
This is due to the several unique features in the AsLOV2, such as the monomeric structure of the protein in both light and dark states and the relatively short transition time between the two states.
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
Constructed infrared difference spectra showed good agreement with experimental transient infrared spectra for EL222 and AsLOV2, permitting assignment of the majority of observed bands.
The good agreement between theory and experiment permitted the assignment of the majority of observed bands
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
The Avena sativa phototropin 1 LOV2 domain is one of the most studied domains for designing photoswitches.
The Light-Oxygen-Voltage 2 (LOV2) domain of Avena Sativa phototropin 1 (AsLOV2) protein is one of the most studied domains in the field of designing photoswitches.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
BLISS activity could be tuned using SpyCatcher variants with different reaction kinetics.
These could be tuned using SpyCatcher variants with different reaction kinetics.
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre can be activated within minutes by blue light illumination without additional chemicals.
LiCre can be activated within minutes of illumination with blue light, without the need of additional chemicals.
activation time within minutes
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in human cells.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light, and in human cells.
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
LiCre was efficient in yeast and enabled light control of β-carotene production.
LiCre was efficient both in yeast, where it allowed us to control the production of β -carotene with light
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
Compared with existing photoactivatable split Cre recombinases, LiCre shows faster and stronger light activation and lower residual dark activity.
When compared to existing photoactivatable Cre recombinases based on two split units, LiCre displayed faster and stronger activation by light as well as a lower residual activity in the dark.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the asLOV2 photoreceptor domain fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the asLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a single flavin-containing protein comprising the AsLOV2 photoreceptor domain fused to a Cre variant with destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant carrying destabilizing mutations in its N-terminal and C-terminal domains.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
LiCre is a novel light-inducible Cre recombinase.
Here, we report the development of LiCre, a novel light-inducible Cre recombinase.
In LOV2, blue light activation leads to formation of a Cys-FMN adduct, rotation of Q513, and unfolding of the Jα helix.
In the C-terminal light-oxygen-voltage (LOV) domain of plant phototropins (LOV2), blue light activation leads to formation of an adduct between a conserved Cys residue and the embedded FMN chromophore, rotation of a conserved Gln (Q513), and unfolding of a helix (Jα-helix)
In LOV2, blue light activation leads to formation of a Cys-FMN adduct, rotation of Q513, and unfolding of the Jα helix.
In the C-terminal light, oxygen, voltage (LOV) domain of plant phototropins (LOV2), blue light activation leads to formation of an adduct between a conserved Cys residue and the embedded FMN chromophore, rotation of a conserved Gln (Q513), and unfolding of a helix (Jα-helix)
In the dark state of AsLOV2, the side chain of N414 is hydrogen bonded to the backbone N-H of Q513.
In the dark state, the side chain of N414 is hydrogen bonded to the backbone N-H of Q513.
Q513 and N414 are critical mediators of protein structural dynamics linking ultrafast FMN excitation to microsecond conformational changes that result in photoreceptor activation and biological function.
Through this multifaceted approach, we show that Q513 and N414 are critical mediators of protein structural dynamics, linking the ultrafast (sub-ps) excitation of the FMN chromophore to the microsecond conformational changes that result in photoreceptor activation and biological function.
conformational change timescale microsecondexcitation timescale sub-ps
Q513 and N414 are critical mediators of protein structural dynamics linking ultrafast FMN excitation to microsecond conformational changes that result in photoreceptor activation and biological function.
Through this multifaceted approach, we show that Q513 and N414 are critical mediators of protein structural dynamics, linking the ultrafast (sub-ps) excitation of the FMN chromophore to the microsecond conformational changes that result in photoreceptor activation and biological function.
Simulations predict that after Cys adduct formation, Q513 undergoes a lever-like motion that disrupts the N414-Q513 backbone interaction and forms a transient side-chain hydrogen bond between Q513 and N414.
The simulations predict a lever-like motion of Q513 after Cys adduct formation resulting in loss of the interaction between the side chain of N414 and the backbone C=O of Q513, and formation of a transient hydrogen bond between the Q513 and N414 side chains.
molecular dynamics simulation duration 7 μcs
Simulations predict that after Cys adduct formation, Q513 undergoes a lever-like motion that disrupts the N414-Q513 backbone interaction and forms a transient side-chain hydrogen bond between Q513 and N414.
The simulations predict a lever-like motion of Q513 after Cys adduct formation resulting in a loss of the interaction between the side chain of N414 and the backbone C═O of Q513, and formation of a transient hydrogen bond between the Q513 and N414 side chains.
In the dark state of AsLOV2, the side chain of N414 is hydrogen bonded to the backbone N-H of Q513.
In the dark state, the side chain of N414 is hydrogen bonded to the backbone N-H of Q513.
Site-directed mutagenesis supports a direct link between Jα helix unfolding dynamics and the cellular function of the Zdk2-AsLOV2 optogenetic construct.
The central role of N414 in signal transduction was evaluated by site-directed mutagenesis supporting a direct link between Jα helix unfolding dynamics and the cellular function of the Zdk2-AsLOV2 optogenetic construct.
Site-directed mutagenesis supports a direct link between Jα helix unfolding dynamics and cellular function of the Zdk2-AsLOV2 optogenetic construct.
The central role of N414 in signal transduction was evaluated by site-directed mutagenesis supporting a direct link between Jα helix unfolding dynamics and the cellular function of the Zdk2-AsLOV2 optogenetic construct.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
LiCre is particularly suited for fundamental research, biomedical research, and controlling industrial bioprocesses.
Given its simplicity and performances, LiCre is particularly suited for fundamental and biomedical research, as well as for controlling industrial bioprocesses.
The N-terminal and C-terminal helices of phototropin LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may support signal integration of LOV1 and LOV2 domains.
It also suggests that the N- and C-terminal helices of phot-LOV2 domains are necessary for allosteric regulation of the phototropin kinase domain and may provide a basis for signal integration of LOV1 and LOV2 domains in phototropins.
The conformational changes in full-length phototropin LOV domains may be smaller than previously assumed, and full unfolding of the Jα helix in AsLOV2 constructs with short A'α helices may be a truncation artifact.
These results are different from shorter constructs, indicating that the conformational changes in full-length phototropin LOV domains might not be as large as previously assumed, and that the well-characterized full unfolding of the Jα helix in AsLOV2 with short A'α helices may be considered a truncation artifact.
In phototropin LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces dissociation and unfolding of the C-terminal Jα helix and the N-terminal A'α helix.
In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α).
Deletion of the A'α helix abolishes light-induced unfolding of the Jα helix in AsLOV2.
Deletion of the A'α helix abolishes the light-induced unfolding of Jα
Extensions of the A'α helix attenuate the light-induced structural change of the Jα helix in AsLOV2.
whereas extensions of the A'α helix lead to an attenuated structural change of Jα
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
Across AsLOV2, YtvA, EL222, and LovK, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved despite differences in tertiary structure.
Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate.
After adduct formation, vibrational spectra and kinetics differ significantly among the full-length LOV photoreceptors and are directly linked to the specific output function of the LOV domain.
However, significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain.
After adduct formation, vibrational spectra and kinetics differ significantly among the full-length LOV photoreceptors and are directly linked to the specific output function of the LOV domain.
However, significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain.
After adduct formation, vibrational spectra and kinetics differ significantly among the full-length LOV photoreceptors and are directly linked to the specific output function of the LOV domain.
However, significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain.
After adduct formation, vibrational spectra and kinetics differ significantly among the full-length LOV photoreceptors and are directly linked to the specific output function of the LOV domain.
However, significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain.
After adduct formation, vibrational spectra and kinetics differ significantly among the full-length LOV photoreceptors and are directly linked to the specific output function of the LOV domain.
However, significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain.
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
The rate of adduct formation varies by only 3.6-fold among the studied LOV proteins.
While the rate of adduct formation varies by only 3.6-fold among the proteins
adduct formation rate variation 3.6 fold
Point mutagenesis testing supports a key mediating role for Q513 in the AsLOV2 allosteric model.
This model is tested through point mutagenesis, elucidating in particular the key mediating role played by Q513.
In AsLOV2, the earliest light-induced events occur in the flavin binding pocket, followed by structural changes in the beta-sheet and then alpha-helix regions, culminating in Jb1-helix unfolding that yields the signaling state.
The earliest events occur in the flavin binding pocket, where a subpicosecond perturbation of the protein matrix occurs. In this perturbed environment, the previously characterized reaction between triplet state isoalloxazine and an adjacent cysteine leads to formation of the adduct state; this step is shown to exhibit dispersive kinetics. This reaction promotes coupling of the optical excitation to successive time-dependent structural changes, initially in the b2-sheet and then b1-helix regions of the AsLOV2 domain, which ultimately gives rise to Jb1-helix unfolding, yielding the signaling state.
Large-scale structural changes in the full-length LOV photoreceptors occur over micro- to submillisecond time scales and vary by orders of magnitude depending on output function.
the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to submillisecond time scales and vary by orders of magnitude depending on the different output function of each LOV domain.
structural change timescale micro- to submillisecondvariation magnitude orders of magnitude
Large-scale structural changes in the full-length LOV photoreceptors occur over micro- to submillisecond time scales and vary by orders of magnitude depending on output function.
the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to submillisecond time scales and vary by orders of magnitude depending on the different output function of each LOV domain.
structural change timescale micro- to submillisecondvariation magnitude orders of magnitude
Large-scale structural changes in the full-length LOV photoreceptors occur over micro- to submillisecond time scales and vary by orders of magnitude depending on output function.
the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to submillisecond time scales and vary by orders of magnitude depending on the different output function of each LOV domain.
structural change timescale micro- to submillisecondvariation magnitude orders of magnitude
Large-scale structural changes in the full-length LOV photoreceptors occur over micro- to submillisecond time scales and vary by orders of magnitude depending on output function.
the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to submillisecond time scales and vary by orders of magnitude depending on the different output function of each LOV domain.
structural change timescale micro- to submillisecondvariation magnitude orders of magnitude
Large-scale structural changes in the full-length LOV photoreceptors occur over micro- to submillisecond time scales and vary by orders of magnitude depending on output function.
the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to submillisecond time scales and vary by orders of magnitude depending on the different output function of each LOV domain.
structural change timescale micro- to submillisecondvariation magnitude orders of magnitude
Time-resolved vibrational spectroscopy coupled with isotope labeling mapped structural evolution of AsLOV2 between 100 fs and 1 ms after optical excitation.
we have mapped the structural evolution of the LOV2 domain of the flavin binding phototropin Avena sativa (AsLOV2) over 10 decades of time, reporting structural dynamics between 100 fs and 1 ms after optical excitation
time window end 1 mstime window start 100 fs
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
The new simulation technique was applied to folding of the C-terminal beta-hairpin fragment of GB1, TrpZip4, and TrpCage, and to conformational changes in signaling of AsLOV2.
We apply this approach on folding of 2 different β-stranded peptides: the C-terminal β-hairpin fragment of GB1 and TrpZip4. Additionally, we use the new simulation technique to study the folding of TrpCage, a small fast folding α-helical peptide. Subsequently, we apply the new methodology on conformation changes in signaling of the light-oxygen voltage (LOV) sensitive domain from Avena sativa (AsLOV2).
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
In dialanine simulations, the two new techniques were compared with conventional REMD for statistical sampling and performance analysis.
In simulations of dialanine, we compare the statistical sampling of the 2 techniques with conventional REMD and analyze their performance.
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
AsLOV2 REST-inhibitory chimeras enabled light-dependent modulation of REST target genes in Neuro2a cells.
By expressing AsLOV2 chimeras in Neuro2a cells, we achieved light-dependent modulation of REST target genes
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
Computational modeling guided fusion of REST-inhibitory domains to AsLOV2.
Computational modeling guided the fusion of the inhibitory domains to the light-sensitive Avena sativa light-oxygen-voltage-sensing (LOV) 2-phototrophin 1 (AsLOV2).
AsLOV2 was used to photocage a peroxisomal targeting sequence, enabling light regulation of peroxisomal protein import.
Here, we used AsLOV2 to photocage a peroxisomal targeting sequence, allowing light regulation of peroxisomal protein import.
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
In primary neurons, light-mediated REST inhibition boosted Na+ currents and neuronal firing.
and boosted Na(+) currents and neuronal firing
The review covers CRY2/CIB1, LOV-domain systems, phytochrome/PIF systems, and Dronpa-based designs as major photosensory modules relevant to optogenetic construct optimization.
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
Light-dependent modulation of REST target genes by AsLOV2 chimeras in Neuro2a cells was associated with improved neural differentiation.
we achieved light-dependent modulation of REST target genes that was associated with an improved neural differentiation
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
In primary neurons, light-mediated REST inhibition increased Na+-channel 1.2 and brain-derived neurotrophic factor transcription.
In primary neurons, light-mediated REST inhibition increased Na(+)-channel 1.2 and brain-derived neurotrophic factor transcription
Some variants with the nearby cysteine moved to alternative locations can still photocycle.
Finally, to investigate the requirements of an active-site cysteine for photocycling, we moved the nearby cysteine to alternative locations and found that some variants can still photocycle.
Dehydration leads to drastically slower LOV photocycle times.
In addition, we demonstrate that dehydration leads to drastically slower photocycle times.
In AsLOV2, the photocycle is accompanied by an allosteric conformational change that activates the attached phototropin kinase in the full-length protein.
In Avena sativa LOV2 (AsLOV2), the photocycle is accompanied by an allosteric conformational change that activates the attached phototropin kinase in the full-length protein.
Mutations at N414 and Q513 identify a potential water gate and H2O coordination sites that affect chromophore electronics and photocycle time by helping catalyze N5 reduction.
Mutations to the N414 and Q513 residues identify a potential water gate and H₂O coordination sites. These residues affect the electronic nature of the chromophore and photocycle time by helping catalyze the N5 reduction leading to the completion of the photocycle.
Reduction of the flavin N5 atom stabilizes both the conformational change and formation of the cysteinyl-flavin adduct in AsLOV2.
Both the conformational change and formation of the cysteinyl-flavin adduct are stabilized by the reduction of the N5 atom in the flavin's isoalloxazine ring.
Electronegative side chains near the chromophore accelerate N5 deprotonation and return to the dark state.
However, electronegative side chains in the vicinity of the chromophore accelerate the N5 deprotonation and the return to the dark state.
Mutating residues that interact with the chromophore isoalloxazine ring to inert functional groups did not fully inhibit the LOV2 photocycle except when the active-site cysteine was mutated.
We mutated all the residues that interact with the chromophore isoalloxazine ring to inert functional groups but none could fully inhibit the photocycle except those to the active-site cysteine.
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
This study concerns elucidation of the photoactivation mechanism of the AsLOV2 domain using accelerated MD simulation.
Accelerated MDシミュレーションを用いたAsLOV2ドメイン光活性機構の解明
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
Mutagenesis and imaging-based screening isolated 12 different AsLOV2 variants with substantially faster thermal reversion kinetics than wild-type AsLOV2.
Based on the mutagenesis and imaging-based screening, we isolated 12 different variants showing substantially faster thermal reversion kinetics than wild-type AsLOV2.
number of faster variants isolated 12
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
With a slight modification of the approach, the authors isolated 8 different decelerated AsLOV2 variants.
With a slight modification of the present approach, we also have efficiently isolated 8 different decelerated variants
number of decelerated variants isolated 8
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416L has a thermal reversion time constant of 4.3 × 10(3) s and is 78-fold slower than wild-type AsLOV2.
represented by AsLOV2-V416L that exhibited thermal reversion with a time constant of 4.3 × 10(3) s (78-fold slower than wild-type AsLOV2).
fold change versus wild-type 78 fold slowerthermal reversion time constant 4.3 × 10(3) s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
AsLOV2-V416T has a thermal reversion time constant of 2.6 s and is 21-fold faster than wild-type AsLOV2.
Among them, AsLOV2-V416T exhibited thermal reversion with a time constant of 2.6 s, 21-fold faster than wild-type AsLOV2.
fold change versus wild-type 21 fold fasterthermal reversion time constant 2.6 s
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
The amino-terminal helix modulates light-activated conformational changes in AsLOV2.
The Amino-Terminal Helix Modulates Light-Activated Conformational Changes in AsLOV2
A weak long-lived emission component from 600 to 650 nm in LOV2 was assigned to phosphorescence from the reactive FMN triplet state.
A weak long-lived component with emission intensity from 600 to 650 nm was assigned to phosphorescence from the reactive FMN triplet state.
emission intensity range 600 to 650 nm
Residues outside the chromophore-binding pocket are important in modulating LOV domain photodynamics.
Taken together, these results demonstrate the importance of residues outside the chromophore-binding pocket in modulating LOV domain photodynamics.
The Avena sativa phototropin 1 LOV2 domain has a fluorescence lifetime of 2.2 ns.
Synchroscan streak camera experiments revealed a fluorescence lifetime of 2.2 ns in LOV2.
fluorescence lifetime 2.2 ns
The fluorescence quantum yield of LOV2 increased from 0.13 to 0.41 when the sample was cooled from 293 K to 77 K.
The fluorescence quantum yield of LOV2 increased from 0.13 to 0.41 upon cooling the sample from 293 to 77 K.
fluorescence quantum yield 0.13fluorescence quantum yield 0.41
The LOV2 triplet state energy level at physiological temperature was determined to be 16600 cm(-1).
This observation allowed determination of the LOV2 triplet state energy level at physiological temperature at 16600 cm(-1).
triplet state energy level 16600 cm(-1)
Phototropin light-dependent action is based on reversible formation of a covalent bond between an FMN cofactor and a conserved cysteine in LOV domains.
The phototropins are blue-light receptors that base their light-dependent action on the reversible formation of a covalent bond between a flavin mononucleotide (FMN) cofactor and a conserved cysteine in light, oxygen or voltage (LOV) domains.
A pronounced phosphorescence emission around 600 nm was observed in the LOV2 domain between 77 and 120 K in steady-state emission.
A pronounced phosphorescence emission around 600 nm was observed in the LOV2 domain between 77 and 120 K in the steady-state emission.
phosphorescence emission wavelength 600 nm
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The intersystem crossing rate is enhanced in LOV2 compared with flavin mononucleotide in solution, likely due to a heavy-atom effect of the nearby conserved cysteine C450.
The ISC rate is enhanced in LOV2 as compared to flavin mononucleotide (FMN) in solution, which likely results from a heavy-atom effect of a nearby conserved cysteine, C450.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
The proximity of the conserved cysteine to FMN enables formation of a covalent adduct between FMN and cysteine and facilitates rapid electronic formation of the reactive FMN triplet state.
The proximity of the cysteine to FMN thus not only enables formation of a covalent adduct between FMN and cysteine, but also facilitates the rapid electronic formation of the reactive FMN triplet state.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
Enhancement of the intersystem crossing rate in LOV2 is induced through weak electron donation by the conserved cysteine, which mixes FMN pi-electrons with heavy sulfur orbitals and manifests as quinoid character in the ground electronic state of oxidized FMN.
Thus, enhancement of the ISC rate in LOV2 is induced through weak electron donation by the cysteine which mixes the FMN pi-electrons with the heavy sulfur orbitals, manifesting itself in a quinoid character of the ground electronic state of oxidized FMN.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In LOV2, the primary photophysical event involves intersystem crossing from the singlet-excited state to the triplet state.
In LOV2, the blue-light sensitive domain of phototropin, the primary photophysical event involves intersystem crossing (ISC) from the singlet-excited state to the triplet state.
In AsLOV2, the conserved glutamine residue Q513 plays a central role in spectral tuning and in signal propagation from the LOV core through the Ibeta strand to the peripheral Jalpha helix.
Together, these data establish that this residue plays a central role in both spectral tuning and signal propagation from the core of the LOV domain through the Ibeta strand to the peripheral Jalpha helix.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Fluorescence line narrowing is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
We demonstrate that FLN is the method of choice to obtain accurate vibrational spectra on highly fluorescent flavoproteins.
Q513L and Q513N mutations in AsLOV2 significantly dampen the structural changes between dark and lit states, producing pseudodark and pseudolit states respectively.
The results show that these mutations significantly dampen the changes between the dark and lit state AsLOV2 structures, leaving the protein in a pseudodark state (Q513L) or a pseudolit state (Q513N).
Q513L and Q513N mutations alter the photochemical properties of AsLOV2, including the lifetime of the photoexcited signaling states.
Further, both mutations changed the photochemical properties of this receptor, in particular the lifetime of the photoexcited signaling states.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
AsLOV2-C450A shows small but significant vibrational spectral shifts relative to wild-type AsLOV2 and Phy3LOV2, including down-shift of Ring I vibrations, upshifts of Ring II and III vibrations, and an upshift of the C2=O mode.
The vibrational spectrum of AsLOV2-C450A showed small but significant shifts with respect to those of wild type AsLOV2 and Phy3LOV2, with a systematic down-shift of Ring I vibrations, upshifts of Ring II and III vibrations and an upshift of the C2=O mode.
Processes other than histidine-mediated base catalysis contribute substantially to adduct thermal decay in AsLOV2.
In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.
Section: abstract
net adduct decay time constant 30 snon histidine decay rate constant (65 s)-1
Processes other than histidine-mediated base catalysis contribute substantially to adduct thermal decay in AsLOV2.
In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.
Section: abstract
net adduct decay time constant 30 snon histidine decay rate constant (65 s)-1
Processes other than histidine-mediated base catalysis contribute substantially to adduct thermal decay in AsLOV2.
In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.
Section: abstract
net adduct decay time constant 30 snon histidine decay rate constant (65 s)-1
Processes other than histidine-mediated base catalysis contribute substantially to adduct thermal decay in AsLOV2.
In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.
Section: abstract
net adduct decay time constant 30 snon histidine decay rate constant (65 s)-1
Processes other than histidine-mediated base catalysis contribute substantially to adduct thermal decay in AsLOV2.
In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.
Section: abstract
net adduct decay time constant 30 snon histidine decay rate constant (65 s)-1
Processes other than histidine-mediated base catalysis contribute substantially to adduct thermal decay in AsLOV2.
In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.
Section: abstract
net adduct decay time constant 30 snon histidine decay rate constant (65 s)-1
Imidazole efficiently enhances dark state recovery of Avena sativa phototropin-1 LOV2 through a base-catalyzed mechanism.
Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism
Section: abstract
acceleration of thermal decay 3 orders of magnitude
Imidazole efficiently enhances dark state recovery of Avena sativa phototropin-1 LOV2 through a base-catalyzed mechanism.
Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism
Section: abstract
acceleration of thermal decay 3 orders of magnitude
Imidazole efficiently enhances dark state recovery of Avena sativa phototropin-1 LOV2 through a base-catalyzed mechanism.
Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism
Section: abstract
acceleration of thermal decay 3 orders of magnitude
Imidazole efficiently enhances dark state recovery of Avena sativa phototropin-1 LOV2 through a base-catalyzed mechanism.
Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism
Section: abstract
acceleration of thermal decay 3 orders of magnitude
Imidazole efficiently enhances dark state recovery of Avena sativa phototropin-1 LOV2 through a base-catalyzed mechanism.
Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism
Section: abstract
acceleration of thermal decay 3 orders of magnitude
Imidazole efficiently enhances dark state recovery of Avena sativa phototropin-1 LOV2 through a base-catalyzed mechanism.
Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism
Section: abstract
acceleration of thermal decay 3 orders of magnitude
Surface histidines in the LOV domain are suggested to act as base catalysts through an unidentified hydrogen-bond network.
Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8.
Section: abstract
histidine mediated base catalysis rate (55 s)-1
Surface histidines in the LOV domain are suggested to act as base catalysts through an unidentified hydrogen-bond network.
Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8.
Section: abstract
histidine mediated base catalysis rate (55 s)-1
Surface histidines in the LOV domain are suggested to act as base catalysts through an unidentified hydrogen-bond network.
Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8.
Section: abstract
histidine mediated base catalysis rate (55 s)-1
Surface histidines in the LOV domain are suggested to act as base catalysts through an unidentified hydrogen-bond network.
Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8.
Section: abstract
histidine mediated base catalysis rate (55 s)-1
Surface histidines in the LOV domain are suggested to act as base catalysts through an unidentified hydrogen-bond network.
Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8.
Section: abstract
histidine mediated base catalysis rate (55 s)-1
Surface histidines in the LOV domain are suggested to act as base catalysts through an unidentified hydrogen-bond network.
Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8.
Section: abstract
histidine mediated base catalysis rate (55 s)-1
The base-catalyzed dark recovery mechanism involves abstraction of the FMN N(5)-H adduct state followed by reprotonation of the reactive cysteine.
via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine
Section: abstract
The base-catalyzed dark recovery mechanism involves abstraction of the FMN N(5)-H adduct state followed by reprotonation of the reactive cysteine.
via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine
Section: abstract
The base-catalyzed dark recovery mechanism involves abstraction of the FMN N(5)-H adduct state followed by reprotonation of the reactive cysteine.
via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine
Section: abstract
The base-catalyzed dark recovery mechanism involves abstraction of the FMN N(5)-H adduct state followed by reprotonation of the reactive cysteine.
via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine
Section: abstract
The base-catalyzed dark recovery mechanism involves abstraction of the FMN N(5)-H adduct state followed by reprotonation of the reactive cysteine.
via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine
Section: abstract
The base-catalyzed dark recovery mechanism involves abstraction of the FMN N(5)-H adduct state followed by reprotonation of the reactive cysteine.
via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine
Section: abstract
The LOV2 crystal structure suggests imidazole may act from a cavity near FMN that is connected to the protein surface by a channel.
The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface.
Section: abstract
The LOV2 crystal structure suggests imidazole may act from a cavity near FMN that is connected to the protein surface by a channel.
The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface.
Section: abstract
The LOV2 crystal structure suggests imidazole may act from a cavity near FMN that is connected to the protein surface by a channel.
The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface.
Section: abstract
The LOV2 crystal structure suggests imidazole may act from a cavity near FMN that is connected to the protein surface by a channel.
The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface.
Section: abstract
The LOV2 crystal structure suggests imidazole may act from a cavity near FMN that is connected to the protein surface by a channel.
The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface.
Section: abstract
The LOV2 crystal structure suggests imidazole may act from a cavity near FMN that is connected to the protein surface by a channel.
The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface.
Section: abstract
Approval Evidence
25 sources69 linked approval claimsfirst-pass slugs aslov2, aslov2-photoreceptor-domain, avena-sativa-aslov2-domain, avena-sativa-lov2, avena-sativa-lov2-phototrophin-1-aslov2, avena-sativa-phototropin-1-light-oxygen-voltage-2-domain, q513a-variant-of-aslov2
blue light activation of the LOV2 (light, oxygen, voltage sensitive) domain of Avena sativa phototropin 1 (AsLOV2)
Source:
дегроном на основе AsLOV2
Source:
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
Source:
Avena sativa phototropin 1 light-oxygen-voltage 2 domain (AsLOV2)
Source:
the paradigmatic LOV2 domain from Avena sativa phototropin 1 (AsLOV2)
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The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein
Source:
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Source:
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2
Source:
Using TiGGER, we determined that upon light activation, the C‐terminus and N‐terminus of AsLOV2 separate in less than 1 s and relax back to equilibrium with a time constant of approximately 60 s.
Source:
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2)
Source:
TiGGER revealed that the light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2
Source:
LiCre is made of a single flavin-containing protein comprising the AsLOV2 photoreceptor domain of Avena sativa fused to a Cre variant
Source:
engineering implicationsupports
The reported hydraulic activation concept offers a new concept for engineering externally controllable protein actuators.
offers a new concept for engineering externally controllable protein actuators
Source:
mechanismsupports
AsLOV2 activation can be initiated by blue light or high pressure and is followed by selective and concerted expulsion of low-entropy, tetrahedrally coordinated wrap water from the protein hydration shell.
we find AsLOV2 activation can be initiated by blue light or high pressure, followed by selective and concerted expulsion of low-entropy, tetrahedrally coordinated "wrap" water from the protein hydration shell
Source:
mechanismsupports
Blue light activation of AsLOV2 gives rise to concerted water movement that induces protein conformational extensions.
This study tests the hypothesis that blue light activation of the LOV2 (light, oxygen, voltage sensitive) domain of Avena sativa phototropin 1 (AsLOV2), gives rise to concerted water movement that induces protein conformational extensions.
Source:
mechanistic interpretationsupports
Interfacial water reshapes the protein free energy landscape during AsLOV2 activation and acts as an active hydraulic fluid driving long-range conformational changes upon light activation.
These findings suggest that interfacial water serves as constituents to reshape the protein's free energy landscape during activation. Our study highlights hydration water as an active hydraulic fluid that can drive long-range conformational changes underlying protein mechanics upon light activation
Source:
topic statementsupports
The paper concerns improvement of the BphP1-QPAS1 system with an AsLOV2-based degron for BIC-light-activated gene expression in plants.
Source:
conformational sequencesupports
AsLOV2 conformational change begins with unfolding of the N-terminal A'α helix in the dark state followed by unfolding of the C-terminal Jα helix.
This conformational change begins with the unfolding of the N-terminal A'α helix in the dark state followed by the unfolding of the C-terminal Jα helix.
Source:
correlation statementsupports
Effects of individual methionine substitutions on signaling-state stability and downstream allosteric responses do not show a clear-cut correlation with redox properties.
Although individual methionine substitutions also affect the stability of the signaling state and downstream allosteric responses, no clear-cut correlation with the redox properties emerges.
Source:
design implicationsupports
Targeted modification of the chromophore environment may mitigate intracellular partial reduction effects and enable design of LOV receptors with stratified redox sensitivities.
The targeted modification of the chromophore environment, as presently demonstrated, may mitigate this effect and enables the design of LOV receptors with stratified redox sensitivities.
Source:
engineering effectsupports
Methionine substitutions near the flavin increase the reduction midpoint potential of AsLOV2 by up to 40 mV.
Replacements of residues at different sites near the flavin by methionine consistently increase E0 from its value of around -280 mV by up to 40 mV.
Source:
functional effectsupports
Methionine introduction impairs photoactivation efficiency and makes AsLOV2 variants less light-sensitive.
methionine introduction invariably impairs photoactivation efficiency and thus renders the resultant AsLOV2 variants less light-sensitive
Source:
hydrogen bond mechanismsupports
Hydrogen bond analyses emphasized roles for the Asn482-Leu453 and Gln479-Val520 hydrogen bonds in the distinct behaviors of the L493A, L496F, Q497A, and D515V AsLOV2 mutants.
In-depth hydrogen bond analyses emphasized the role of two hydrogen bonds, Asn482-Leu453 and Gln479-Val520, in the observed distinct behaviors of L493A, L496F, Q497A, and D515V mutants.
Source:
measured propertysupports
AsLOV2 has a reduction midpoint potential near -280 mV.
With a reduction midpoint potential near -280 mV, AsLOV2
Source:
mechanistic rolesupports
In AsLOV2, beta-sheets are crucial components mediating allosteric signal transmission between the two termini.
In this photoreceptor, β-sheets are identified as crucial components for mediating allosteric signal transmission between the two termini.
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mechanistic rolesupports
The Hβ and Iβ strands are the most critical and influential beta-sheets in AsLOV2's allosteric mechanism.
Through combined experimental and computational investigations, the Hβ and Iβ strands are recognized as the most critical and influential β-sheets in AsLOV2's allosteric mechanism.
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use casesupports
AsLOV2-based optogenetic tools are used for actin imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging
Source:
application relevancesupports
The reported mechanistic insights are useful for enhancing the performance of AsLOV2-based photoswitches.
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
Source:
comparative observationsupports
The light-activated long-range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated with similarly slowed relaxation of the optically excited chromophore.
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
mechanismsupports
Blue light exposure causes unfolding of the C-terminal Jα-helix in AsLOV2.
The C terminal Jα-helix of the Avena Sativa’s Light Oxygen and Voltage (AsLOV2) protein, unfolds on exposure to blue light.
Source:
mechanismsupports
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Source:
mechanismsupports
Displacement of N492 out of the FMN binding pocket is essential for initiation of AsLOV2 Jα-helix unfolding and does not necessarily require Q513.
the displacement of N492 out of the FMN binding pocket, not necessarily requiring Q513, is essential for the initiation of the Jα-helix unfolding
Source:
Comparisons
Source-backed strengths
Mechanistic studies support a defined activation process in which blue light induces concerted water movement, hydration-shell water expulsion, and long-range conformational extension. Additional evidence indicates a specific conformational sequence, with unfolding beginning at the N-terminal A'α helix and followed by the C-terminal Jα helix, which provides a structurally interpretable basis for engineering. The literature set also indicates multiple engineering routes around the domain, including circular permutation, mutational tuning, and screening of LOV kinetic variants.
Source:
offers a new concept for engineering externally controllable protein actuators
Source:
Replacements of residues at different sites near the flavin by methionine consistently increase E0 from its value of around -280 mV by up to 40 mV.
Source:
TiGGER revealed that the light‐activated long‐range mechanical motion is slowed in the Q513A variant of AsLOV2 and is correlated to the similarly slowed relaxation of the optically excited chromophore as described in recent literature.
Source:
we inserted the photosensor light-oxygen-voltage-sensing domain 2 of <i>Avena sativa</i> (AsLOV2) into selected sites of isocitrate dehydrogenase (IDH) ... to construct photoswitchable IDH-AsLOV2 (ILOVs)
Compared with Avena sativa phototropin-1 LOV2 domain
AsLOV2 and Avena sativa phototropin-1 LOV2 domain address a similar problem space because they share recombination, signaling.
Shared frame: same top-level item type; shared target processes: recombination, signaling; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Strengths here: appears more independently replicated; may reduce component-count burden.
Compared with BcLOV4 photoreceptor
AsLOV2 and BcLOV4 photoreceptor address a similar problem space because they share localization, recombination, signaling.
Shared frame: same top-level item type; shared target processes: localization, recombination, signaling; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice; may reduce component-count burden.
Compared with SspB
AsLOV2 and SspB address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Strengths here: appears more independently replicated; may reduce component-count burden.
Ranked Citations
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- 17.StructuralSource 17Proceedings of the National Academy of Sciences2015Claim 1153Claim 1154Claim 1154
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Curation Status
Seed dossier — not yet curator-complete
- Validation rollups and replication scores are pending ingestion
- Citation list may be incomplete or contain placeholders
- Observation table will populate once evidence is curated