Reliable protein folding on non-funneled energy landscapes: the free energy reaction path

Details Reliable protein folding on non-funneled energy landscapes: the free energy reaction path Reliable protein folding on non-funneled energy landscapes: the free energy reaction path

2008-02-01

arxiv.org/abs/0802.0209v1

Biophys. J. 95, 2692 (2008)

Biology

Quantitative Biology

Biomolecules

13 pages, 9 figures

Scientific paper

10.1529/biophysj.108.133132

A theoretical framework is developed to study the dynamics of protein folding. The key insight is that the search for the native protein conformation is influenced by the rate r at which external parameters, such as temperature, chemical denaturant or pH, are adjusted to induce folding. A theory based on this insight predicts that (1) proteins with non-funneled energy landscapes can fold reliably to their native state, (2) reliable folding can occur as an equilibrium or out-of-equilibrium process, and (3) reliable folding only occurs when the rate r is below a limiting value, which can be calculated from measurements of the free energy. We test these predictions against numerical simulations of model proteins with a single energy scale.

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