Structural basis of folding cooperativity in model proteins: insights from a microcanonical perspective.

ABSTRACT: Two-state cooperativity is an important characteristic in protein folding. It is defined by a depletion of states that lie energetically between folded and unfolded conformations. There are different ways to test for two-state cooperativity; however, most of these approaches probe indirect proxies of this depletion. Generalized-ensemble computer simulations allow us to unambiguously identify this transition by a microcanonical analysis on the basis of the density of states. Here, we present a detailed characterization of several helical peptides obtained by coarse-grained simulations. The level of resolution of the coarse-grained model allowed to study realistic structures ranging from small α-helices to a de novo three-helix bundle without biasing the force field toward the native state o

SUBMITTER: Bereau T 

PROVIDER: S-EPMC3117192 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature