Accurate Protein-Folding Transition-Path Statistics from a Simple Free-Energy Landscape.

ABSTRACT: A central goal of protein-folding theory is to predict the stochastic dynamics of transition paths-the rare trajectories that transit between the folded and unfolded ensembles-using only thermodynamic information, such as a low-dimensional equilibrium free-energy landscape. However, commonly used one-dimensional landscapes typically fall short of this aim, because an empirical coordinate-dependent diffusion coefficient has to be fit to transition-path trajectory data in order to reproduce the transition-path dynamics. We show that an alternative, first-principles free-energy landscape predicts transition-path statistics that agree well with simulations and single-molecule experiments without requiring dynamical data as an input. This "topological configuration" model assumes that distinct,

SUBMITTER: Jacobs WM 

PROVIDER: S-EPMC6386633 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature