Insights into Actin Polymerization and Nucleation Using a Coarse-Grained Model.

ABSTRACT: We studied actin filament polymerization and nucleation with molecular dynamics simulations and a previously established coarse-grained model having each residue represented by a single interaction site located at the C_α atom. We approximate each actin protein as a fully or partially rigid unit to identify the equilibrium structural ensemble of interprotein complexes. Monomers in the F-actin configuration bound to both barbed and pointed ends of a short F-actin filament at the anticipated locations for polymerization. Binding at both ends occurred with similar affinity. Contacts between residues of the incoming subunit and the short filament were consistent with expectation from models based on crystallography, x-ray diffraction, and cryo-electron microscopy. Binding at the barb

SUBMITTER: Horan BG 

PROVIDER: S-EPMC7399502 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature