Competing interactions give rise to two-state behavior and switch-like transitions in charge-rich intrinsically disordered proteins.

ABSTRACT: The most commonly occurring intrinsically disordered proteins (IDPs) are polyampholytes, which are defined by the duality of low net charge per residue and high fractions of charged residues. Recent experiments have uncovered nuances regarding sequence–ensemble relationships of model polyampholytic IDPs. These include differences in conformational preferences for sequences with lysine vs. arginine and the suggestion that well-mixed sequences form a range of conformations, including globules, conformations with ensemble averages that are reminiscent of ideal chains, or self-avoiding walks. Here, we explain these observations by analyzing results from atomistic simulations. We find that polyampholytic IDPs generally sample two distinct stable states, namely, globules and self-avoiding walks.

SUBMITTER: Zeng X 

PROVIDER: S-EPMC9171777 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature