Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments.

ABSTRACT: Actin filaments continually assemble and disassemble within a cell. Assembled filaments "age" as a bound nucleotide ATP within each actin subunit quickly hydrolyzes followed by a slower release of the phosphate P_i, leaving behind a bound ADP. This subtle change in nucleotide state of actin subunits affects filament rigidity as well as its interactions with binding partners. We present here a systematic multiscale ultra-coarse-graining approach that provides a computationally efficient way to simulate a long actin filament undergoing ATP hydrolysis and phosphate-release reactions while systematically taking into account available atomistic details. The slower conformational changes and their dependence on the chemical reactions are simulated with the ultra-coarse-graining model b

SUBMITTER: Katkar HH 

PROVIDER: S-EPMC6260209 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature