Complex intramolecular mechanics of G-actin--an elastic network study.

ABSTRACT: Systematic numerical investigations of conformational motions in single actin molecules were performed by employing a simple elastic-network (EN) model of this protein. Similar to previous investigations for myosin, we found that G-actin essentially behaves as a strain sensor, responding by well-defined domain motions to mechanical perturbations. Several sensitive residues within the nucleotide-binding pocket (NBP) could be identified, such that the perturbation of any of them can induce characteristic flattening of actin molecules and closing of the cleft between their two mobile domains. Extending the EN model by introduction of a set of breakable links which become effective only when two domains approach one another, it was observed that G-actin can possess a metastable state correspon

SUBMITTER: Duttmann M 

PROVIDER: S-EPMC3471905 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature