The role of high-dimensional diffusive search, stabilization, and frustration in protein folding.

ABSTRACT: Proteins are polymeric molecules with many degrees of conformational freedom whose internal energetic interactions are typically screened to small distances. Therefore, in the high-dimensional conformation space of a protein, the energy landscape is locally relatively flat, in contrast to low-dimensional representations, where, because of the induced entropic contribution to the full free energy, it appears funnel-like. Proteins explore the conformation space by searching these flat subspaces to find a narrow energetic alley that we call a hypergutter and then explore the next, lower-dimensional, subspace. Such a framework provides an effective representation of the energy landscape and folding kinetics that does justice to the essential characteristic of high-dimensionality of the search-

SUBMITTER: Rimratchada S 

PROVIDER: S-EPMC4008833 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature