Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) are ensembles of interconverting conformers whose conformational properties are governed by several physico-chemical factors, including their amino acid composition and the arrangement of oppositely charged residues within the primary structure. In this work, we investigate the effects of charge patterning on the average compactness and shape of three model IDPs with different proline content. We model IDP ensemble conformations as ellipsoids, whose size and shape are calculated by combining data from size-exclusion chromatography and native mass spectrometry. For each model IDP, we analyzed the wild-type protein and two synthetic variants with permuted positions of charged residues, where positive and negative amino acids are either evenly distribu

SUBMITTER: Bianchi G 

PROVIDER: S-EPMC9031945 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature