Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.

ABSTRACT: As theory and experiment have shown, protein dehydration is a major contributor to protein folding. Dehydration upon folding can be characterized directly by all-atom simulations of fast pressure drops, which create desolvated pockets inside the nascent hydrophobic core. Here, we study pressure-drop refolding of three λ-repressor fragment (λ_6-85) mutants computationally and experimentally. The three mutants report on tertiary structure formation via different fluorescent helix-helix contact pairs. All-atom simulations of pressure drops capture refolding and unfolding of all three mutants by a similar mechanism, thus validating the nonperturbative nature of the fluorescent contact probes. Analysis of simulated interprobe distances shows that the α-helix 1-3 pair distance displays

SUBMITTER: Prigozhin MB 

PROVIDER: S-EPMC6431218 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature