Mutational scan inferred binding energetics and structure in intrinsically disordered protein CcdA.

ABSTRACT: Unlike globular proteins, mutational effects on the function of Intrinsically Disordered Proteins (IDPs) are not well-studied. Deep Mutational Scanning of a yeast surface displayed mutant library yields insights into sequence-function relationships in the CcdA IDP. The approach enables facile prediction of interface residues and local structural signatures of the bound conformation. In contrast to previous titration-based approaches which use a number of ligand concentrations, we show that use of a single rationally chosen ligand concentration can provide quantitative estimates of relative binding constants for large numbers of protein variants. This is because the extended interface of IDP ensures that energetic effects of point mutations are spread over a much smaller range than for glob

SUBMITTER: Chandra S 

PROVIDER: S-EPMC9951195 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature