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Reliable protein folding on complex energy landscapes: the free energy reaction path



Reliable protein folding on complex energy landscapes: the free energy reaction path



Biophysical Journal 95(6): 2692-2701



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 complex 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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Accession: 055479875

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PMID: 18515400

DOI: 10.1529/biophysj.108.133132


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