Diffusive Dynamics of Contact Formation in Disordered Polypeptides.

ABSTRACT: Experiments measuring contact formation between probes in disordered chains provide information on the fundamental time scales relevant to protein folding. However, their interpretation usually relies on one-dimensional (1D) diffusion models, as do many experiments probing a single distance. Here, we use all-atom molecular simulations to capture both the time scales of contact formation, as well as the scaling with peptide length for tryptophan triplet quenching experiments, revealing the sensitivity of the experimental quenching times to the configurational space explored by the chain. We find a remarkable consistency between the results of the full calculation and from Szabo-Schulten-Schulten theory applied to a 1D diffusion model, supporting the validity of such models. The significant

SUBMITTER: Zerze GH 

PROVIDER: S-EPMC5578460 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature