The elastic properties of the structurally characterized myosin II S2 subdomain: a molecular dynamics and normal mode analysis.

ABSTRACT: The elastic properties (stretching and bending moduli) of myosin are expected to play an important role in its function. Of particular interest is the extended alpha-helical coiled-coil portion of the molecule. Since there is no high resolution structure for the entire coiled-coil, a study is made of the scallop myosin II S2 subdomain for which an x-ray structure is available (Protein Data Bank 1nkn). We estimate the stretching and bending moduli of the S2 subdomain with an atomic level model by use of molecular simulations. Results were obtained from nonequilibrium molecular dynamics simulations in the presence of an external force, from the fluctuations in equilibrium molecular dynamics simulations and from normal modes. In addition, a poly-Ala (78 amino acid residues) alpha-helix model

SUBMITTER: Adamovic I 

PROVIDER: S-EPMC2367198 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature