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Biophys J, November 2000, p. 2722-2727, Vol. 79, No. 5

Pathways in Two-State Protein Folding

Audun Bakk,* Johan S. Høye,* Alex Hansen,dagger Kim Sneppen,dagger and Mogens H. JensenDagger

 *Department of Physics, Norwegian University of Science and Technology, NTNU, N-7491 Trondheim, Norway;  dagger International Center for Condensed Matter Physics, University of Brasília, 70919-970 Brasília-DF, Brazil; and  Dagger Niels Bohr Institute, DK-2100 Copenhagen, Denmark

Thermodynamic measurements of proteins indicate that the folding to the native state takes place either through stable intermediates or through a two-state process without intermediates. The rather short folding times of proteins indicate that folding is guided through some sequence of contact bindings. We discuss the possibility of reconciling a two-state folding event with a sequential folding process in a schematic model of protein folding. We propose a new dynamical transition temperature that is lower than the temperature at which proteins in equilibrium unfold. This is in qualitative agreement with observations of in vivo protein folding activity quantified by chaperone concentration in Escherichia coli. Finally, we discuss our framework in connection with the unfolding of proteins at low temperatures.

Biophys J, November 2000, p. 2722-2727, Vol. 79, No. 5
© 2000 by the Biophysical Society   0006-3495/00/11/2722/06  $2.00




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