Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.

ABSTRACT: The actin filament network is in part remodeled by the action of a family of filament severing proteins that are responsible for modulating the ratio between monomeric and filamentous actin. Recent work on the protein actophorin from the amoeba Acanthamoeba castellani identified a series of site-directed mutations that increase the thermal stability of the protein by 22°C. Here, we expand this observation by showing that the mutant protein is also significantly stable to both equilibrium and kinetic chemical denaturation, and employ computer simulations to account for the increase in thermal or chemical stability through an accounting of atomic-level interactions. Specifically, the potential of mean force (PMF) can be obtained from steered molecular dynamics (SMD) simulations in which a pr

SUBMITTER: Thota N 

PROVIDER: S-EPMC10398266 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature