Mechanochemical Coupling in the Myosin Motor Domain. II. Analysis of Critical Residues

@article{Yu2007MechanochemicalCI,
  title={Mechanochemical Coupling in the Myosin Motor Domain. II. Analysis of Critical Residues},
  author={Haibo Yu and Liang Ma and Y. Yang and Q. Cui},
  journal={PLoS Computational Biology},
  year={2007},
  volume={3}
}
An important challenge in the analysis of mechanochemical coupling in molecular motors is to identify residues that dictate the tight coupling between the chemical site and distant structural rearrangements. In this work, a systematic attempt is made to tackle this issue for the conventional myosin. By judiciously combining a range of computational techniques with different approximations and strength, which include targeted molecular dynamics, normal mode analysis, and statistical coupling… Expand
Mechanochemical Coupling in the Myosin Motor Domain. I. Insights from Equilibrium Active-Site Simulations
Mechanical coupling in myosin V: a simulation study.
Actomyosin Interaction: Mechanical and Energetic Properties in Different Nucleotide Binding States
Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.
Mechanical Network in Titin Immunoglobulin from Force Distribution Analysis
Allostery Wiring Map for Kinesin Energy Transduction and Its Evolution*
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 106 REFERENCES
The Myosin Relay Helix to Converter Interface Remains Intact throughout the Actomyosin ATPase Cycle*
Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.
Evidence for cleft closure in actomyosin upon ADP release
The Structural Basis of the Myosin ATPase Activity*
  • I. Rayment
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 1996
...
1
2
3
4
5
...