Exploring protein-folding ensembles: a variable-barrier model for the analysis of equilibrium unfolding experiments.

ABSTRACT: Recent theoretical and experimental results point to the existence of small barriers to protein folding. These barriers can even be absent altogether, resulting in a continuous folding transition (i.e., downhill folding). With small barriers, the detailed properties of folding ensembles may become accessible to equilibrium experiments. However, further progress is hampered because folding experiments are interpreted with chemical models (e.g., the two-state model), which assume the existence of well defined macrostates separated by arbitrarily high barriers. Here we introduce a phenomenological model based on the classical Landau theory for critical transitions. In this physical model the height of the thermodynamic free energy barrier and the general properties of the folding ensemble are

SUBMITTER: Munoz V 

PROVIDER: S-EPMC539728 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature