Pathways in Two-State Protein Folding

Details Pathways in Two-State Protein Folding Pathways in Two-State Protein Folding

1999-12-30

arxiv.org/abs/cond-mat/9912483v1

Physics

Condensed Matter

4 pages RevTeX, 5 Postscript figure

Scientific paper

10.1016/S0006-3495(00)76510-6

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.

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