How a highly acidic SH3 domain folds in the absence of its charged peptide target.

ABSTRACT: Charged residues on the surface of proteins are critical for both protein stability and interactions. However, many proteins contain binding regions with a high net charge that may destabilize the protein but are useful for binding to oppositely charged targets. We hypothesized that these domains would be marginally stable, as electrostatic repulsion would compete with favorable hydrophobic collapse during folding. Furthermore, by increasing the salt concentration, we predict that these protein folds would be stabilized by mimicking some of the favorable electrostatic interactions that take place during target binding. We varied the salt and urea concentrations to probe the contributions of electrostatic and hydrophobic interactions for the folding of the yeast SH3 domain found in Abp1p. T

SUBMITTER: Jaramillo-Martinez V 

PROVIDER: S-EPMC10108434 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature