Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins.

ABSTRACT: The stability and physiological function of many biomolecular coacervates depend on the structure and dynamics of intrinsically disordered proteins (IDPs) that typically contain a significant fraction of charged residues. Although the effect of relative arrangement of charged residues on IDP conformation is a well-studied problem, the associated changes in dynamics are far less understood. In this work, we systematically interrogate the effects of charge distribution on the chain-level and segmental dynamics of polyampholytic IDPs in dilute solutions. We study a coarse-grained model polyampholyte consisting of an equal fraction of two oppositely charged residues (glutamic acid and lysine) that undergoes a transition from an ideal chain-like conformation for uniformly charge-patterned seque

SUBMITTER: Devarajan DS 

PROVIDER: S-EPMC10798675 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature