Hydrophobic association of alpha-helices, steric dewetting, and enthalpic barriers to protein folding.

ABSTRACT: Efficient protein folding implies a microscopic funnel-like multidimensional free-energy landscape. Macroscopically, conformational entropy reduction can manifest itself as part of an empirical barrier in the traditional view of folding, but experiments show that such barriers can also entail significant unfavorable enthalpy changes. This observation raises the puzzling possibility, irrespective of conformational entropy, that individual microscopic folding trajectories may encounter large uphill moves and thus the multidimensional free-energy landscape may not be funnel-like. Here, we investigate how nanoscale hydrophobic interactions might underpin this salient enthalpic effect in biomolecular assembly by computer simulations of the association of two preformed polyalanine or polyleucine

SUBMITTER: MacCallum JL 

PROVIDER: S-EPMC1847460 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature