A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy.

ABSTRACT: For small molecule reaction kinetics, computed reaction coordinates often mimic experimentally measured observables quite accurately. Although nowadays simulated and measured biomolecule kinetics can be compared on the same time scale, a gap between computed and experimental observables remains. Here we directly compared temperature-jump experiments and molecular dynamics simulations of protein folding dynamics using the same observable: the time-dependent infrared spectrum. We first measured the stability and folding kinetics of the fastest-folding β-protein, the GTT35 WW domain, using its structurally specific infrared spectrum. The relaxation dynamics of the peptide backbone, β-sheets, turn, and random coil were measured independently by probing the amide I' region at different frequenc

SUBMITTER: Davis CM 

PROVIDER: S-EPMC6301204 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature