Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.

ABSTRACT: Much attention is being paid to conformational biases in the ensembles of intrinsically disordered proteins. However, it is currently unknown whether or how conformational biases within the disordered ensembles of foldable proteins affect function in vivo. Recently, we demonstrated that water can be a good solvent for unfolded polypeptide chains, even those with a hydrophobic and charged sequence composition typical of folded proteins. These results run counter to the generally accepted model that protein folding begins with hydrophobicity-driven chain collapse. Here we investigate what other features, beyond amino acid composition, govern chain collapse. We found that local clustering of hydrophobic and/or charged residues leads to significant collapse of the unfolded ensemble of pertacti

SUBMITTER: Bowman MA 

PROVIDER: S-EPMC7519328 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature