Differences in internal dynamics of actin under different structural states detected by neutron scattering.

ABSTRACT: F-actin, a helical polymer formed by polymerization of the monomers (G-actin), plays crucial roles in various aspects of cell motility. Flexibility of F-actin has been suggested to be important for such a variety of functions. Understanding the flexibility of F-actin requires characterization of a hierarchy of dynamical properties, from internal dynamics of the actin monomers through domain motions within the monomers and relative motions between the monomers within F-actin to large-scale motions of F-actin as a whole. As a first step toward this ultimate purpose, we carried out elastic incoherent neutron scattering experiments on powders of F-actin and G-actin hydrated with D(2)O and characterized the internal dynamics of F-actin and G-actin. Well established techniques and analysis enabl

SUBMITTER: Fujiwara S 

PROVIDER: S-EPMC2397340 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature