Capillarity-like growth of protein folding nuclei.

ABSTRACT: A full structural description of transition state ensembles in protein folding includes the specificity of the ordered residues composing the folding nucleus as well as spatial density. To our knowledge, the spatial properties of the folding nucleus and interface of specific nuclei have yet to receive significant attention. We analyze folding routes predicted by a variational model in terms of a generalized formalism of the capillarity scaling theory that assumes the volume of the folded core of the nucleus grows with chain length as V(f) approximately N(3nu). For 27 two-state proteins studied, the scaling exponent nu ranges from 0.2 to 0.45 with an average of 0.33. This average value corresponds to packing of rigid objects, although generally the effective monomer size in the folded core

SUBMITTER: Qi X 

PROVIDER: S-EPMC2516257 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature