Mechanochemical coupling in the myosin motor domain. II. Analysis of critical residues.

ABSTRACT: 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 analysis, we are able to identify a set of important residues and propose their relevant function during the recovery stroke of myosin. These analyses also allowed us to make connections with previous experimental and computational studies in a critical manner. The behavior of the widely used reporter r

SUBMITTER: Yu H 

PROVIDER: S-EPMC1800309 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature