Source 1primary paper2023
Toolkit/Molecular Dynamic simulations
Molecular Dynamic simulations
Also known as: MD simulations
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Molecular dynamics simulations combined with Markov state modeling were used to characterize blue-light-induced conformational switching in the Avena sativa LOV2 (AsLOV2) domain. This computation method resolved C-terminal Jα-helix unfolding into seven structurally distinguishable steps spanning initiation and post-initiation phases.
Usefulness & Problems
Why this is useful
This method is useful for extracting mechanistic, state-resolved models of AsLOV2 photoswitch activation from simulation data. The reported insights were described as relevant for enhancing the performance of AsLOV2-based photoswitches.
Source:
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
Problem solved
It addresses the problem of defining how blue light triggers stepwise Jα-helix unfolding in AsLOV2 at structural resolution. Specifically, it decomposes the unfolding pathway into discrete states and links them to interaction-cascade collapse, Q513 reorientation, and disruption of hydrophobic contacts with the Iβ-sheet.
Source:
Overall, the study provides insights useful to enhance the performance of AsLOV2 based photoswitches.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete computational method used to design, rank, or analyze an engineered system.
Mechanisms
hydrophobic interaction disruptioninteraction-cascade collapselight-induced conformational switchingmarkov state decomposition of conformational transitionsstepwise helix unfoldingTarget processes
No target processes tagged yet.
Implementation Constraints
The reported implementation used molecular dynamics simulations together with a Markov state modeling approach. The evidence ties the method to the AsLOV2 blue-light response and FMN-centered interaction network, but it does not specify force fields, simulation lengths, software, or hardware.
The supplied evidence supports mechanistic interpretation in AsLOV2 but does not document broader benchmarking, predictive accuracy, or application to other systems. Independent replication is not provided in the supplied evidence, and practical computational requirements are not described.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
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.
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
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
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 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
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 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.
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.
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.
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.
number of unfolding steps 7
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 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
Approval Evidence
1 source3 linked approval claimsfirst-pass slug molecular-dynamic-simulations
Using Molecular Dynamic (MD) simulations
Source:
Using Molecular Dynamic (MD) simulations and the Markov State Modeling (MSM) approach we provide the mechanism that explains the stepwise unfolding of the Jα-helix.
Source:
mechanismsupports
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.
Source:
mechanismsupports
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.
Source:
mechanismsupports
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.
Source:
Comparisons
Source-backed strengths
The method produced a seven-step structural model of Jα-helix unfolding with distinct initiation and post-initiation phases. It identified specific mechanistic features, including collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade, essential displacement of N492 from the FMN pocket, Q513-dependent crossing of a hydrophobic barrier, and breaking of hydrophobic interactions between the Jα-helix and Iβ-sheet.
Ranked Citations
- 1.