Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.

ABSTRACT: Molecular fluctuations directly reflect the underlying energy landscape. Variance analysis examines protein dynamics in several biochemistry-driven approaches, yet measurement of probe-independent fluctuations in proteins exposed to mechanical forces remains only accessible through steered molecular dynamics simulations. Using single molecule magnetic tweezers, here we conduct variance analysis to show that individual unfolding and refolding transitions occurring in dynamic equilibrium in a single protein under force are hallmarked by a change in the protein's end-to-end fluctuations, revealing a change in protein stiffness. By unfolding and refolding three structurally distinct proteins under a wide range of constant forces, we demonstrate that the associated change in protein compliance

SUBMITTER: Stannard A 

PROVIDER: S-EPMC7610714 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature