Microscopic interpretation of folding ϕ-values using the transition path ensemble.

ABSTRACT: All-atom molecular dynamics simulations now allow us to create movies of proteins folding and unfolding. However, it is difficult to assess the accuracy of the folding mechanisms observed because experiments cannot yet directly resolve events occurring along the transition paths between unfolded and folded states. Protein folding ϕ-values provide residue-resolved information about folding mechanisms by comparing the effects of mutations on folding rates and stability, but determining ϕ-values by separately simulating mutant proteins would be computationally demanding and prone to large statistical errors. Here we use transition path theory to develop a method for computing ϕ-values directly from the transition path ensemble, without the need for additional simulations. This path-based appr

SUBMITTER: Best RB 

PROVIDER: S-EPMC4812701 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature