Nonlinearity of mechanochemical motions in motor proteins.

ABSTRACT: The assumption of linear response of protein molecules to thermal noise or structural perturbations, such as ligand binding or detachment, is broadly used in the studies of protein dynamics. Conformational motions in proteins are traditionally analyzed in terms of normal modes and experimental data on thermal fluctuations in such macromolecules is also usually interpreted in terms of the excitation of normal modes. We have chosen two important protein motors--myosin V and kinesin KIF1A--and performed numerical investigations of their conformational relaxation properties within the coarse-grained elastic network approximation. We have found that the linearity assumption is deficient for ligand-induced conformational motions and can even be violated for characteristic thermal fluctuations. T

SUBMITTER: Togashi Y 

PROVIDER: S-EPMC2887453 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature