Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.

ABSTRACT: It has become increasingly evident that the conformational distributions of intrinsically disordered proteins or regions are strongly dependent on their amino acid compositions and sequence. To facilitate a systematic investigation of these sequence-ensemble relationships, we selected a set of 16 naturally occurring intrinsically disordered regions of identical length but with large differences in amino acid composition, hydrophobicity, and charge patterning. We probed their conformational ensembles with single-molecule Förster resonance energy transfer (FRET), complemented by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy as well as small-angle X-ray scattering (SAXS). The set of disordered proteins shows a strong dependence of the chain dimensions on sequence c

SUBMITTER: Holla A 

PROVIDER: S-EPMC11672150 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature