Pathways in Two-State Protein Folding

Abstract

The thermodynamics of proteins indicate that folding/unfolding takes place either through stable intermediates or through a two-state process without intermediates. The rather short folding times of the two-state process indicate that folding is guided. We reconcile these two seemingly contradictory observations quantitatively in a schematic model of protein folding. We propose a new dynamical transition temperature which is lower than the thermodynamic one, in qualitative agreement with in vivo measurement of protein stability using E.coli. Finally we demonstrate that our framework is easily generalized to encompass cold unfolding, and make predictions that relate the sharpness of the cold and hot unfolding transitions.

4 pages RevTeX, 5 Postscript figure

References in corpus (2)

• Statistical mechanics of warm and cold unfolding in proteins
• Thermodynamics of Heat Shock Response

Cited by in corpus (5)

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• Heat Capacity of Protein Folding
• A protein model exhibiting three folding transitions
• Specific Heat upon Aqueous Unfolding of the Protein Interior: A Theoretical Approach
• Solvation Effects and Driving Forces for Protein Thermodynamic And Kinetic Cooperativity: How Adequate Is Native-Centric Topological Modeling?