Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.

ABSTRACT: Although folded proteins are commonly depicted as simplistic combinations of β-strands and α-helices, the actual properties and functions of these secondary-structure elements in their native contexts are just partly understood. The principal reason is that the behavior of individual β- and α-elements is obscured by the global folding cooperativity. In this study, we have circumvented this problem by designing frustrated variants of the mixed α/β-protein S6, which allow the structural behavior of individual β-strands and α-helices to be targeted selectively by stopped-flow kinetics, X-ray crystallography, and solution-state NMR. Essentially, our approach is based on provoking intramolecular "domain swap." The results show that the α- and β-elements have quite different characteristics: The

SUBMITTER: Wang H 

PROVIDER: S-EPMC7682573 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature