Source 1primary paper2023
Toolkit/Markov State Modeling
Markov State Modeling
Also known as: MSM
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Markov State Modeling (MSM) is a computational method applied with molecular dynamics simulations to resolve conformational dynamics in the AsLOV2 photosensory domain. In the cited 2023 study, MSM was used to explain blue-light-induced stepwise unfolding of the C-terminal Jα-helix and to identify seven structurally distinguishable unfolding states spanning initiation and post-initiation phases.
Usefulness & Problems
Why this is useful
MSM is useful for extracting discrete mechanistic states and transition structure from molecular dynamics trajectories of light-responsive proteins. In this case, the resulting mechanistic insights were reported as useful 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
This method addresses the problem of resolving how blue light drives the AsLOV2 C-terminal Jα-helix through a multistep unfolding process that is difficult to interpret directly from raw simulation trajectories. The cited work used MSM to decompose this process into initiation and post-initiation phases with specific structural events.
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
light-induced allosteric switchingstate decomposition of conformational dynamicsstepwise conformational unfoldingTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The reported implementation combined molecular dynamics simulations with Markov State Modeling. The biological context was the blue-light-responsive AsLOV2 domain containing an FMN binding pocket and a C-terminal Jα-helix, but the supplied evidence does not provide workflow parameters, software details, state construction settings, or sampling requirements.
The evidence is limited to a single 2023 study focused on AsLOV2 and does not establish general performance across other proteins or photoswitch systems. The supplied evidence does not report experimental validation of the inferred states, quantitative predictive accuracy, or benchmarking against alternative computational approaches.
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.
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.
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.
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
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 source6 linked approval claimsfirst-pass slug markov-state-modeling
and the Markov State Modeling (MSM) approach
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:
mechanistic modelsupports
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
Source:
method resultsupports
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
Source:
method resultsupports
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
Source:
Comparisons
Source-backed strengths
The study reports that MSM resolved seven structurally distinguishable steps in AsLOV2 Jα-helix unfolding. It also linked these states to specific structural features, including collapse of the FMN-Q513-N492-L480-W491-Q479-V520-A524 interaction cascade, displacement of N492 from the FMN pocket, and reorientation of Q513 during crossing of a hydrophobic barrier.
Ranked Citations
- 1.