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The Complex Kinetics of Protein Folding in Wide Temperature Ranges

State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, People's Republic of China; and The Department of Chemistry and Department of Physics, State University of New York, Stony Brook, New York

Correspondence: Address reprint requests to Jin Wang, E-mail: jinwang{at}sprynet.com.

The complex protein folding kinetics in wide temperature ranges is studied through diffusive dynamics on the underlying energy landscape. The well-known kinetic chevron rollover behavior is recovered from the mean first passage time, with the U-shape dependence on temperature. The fastest folding temperature T₀ is found to be smaller than the folding transition temperature T_f. We found that the fluctuations of the kinetics through the distribution of first passage time show rather universal behavior, from high-temperature exponential Poissonian kinetics to the relatively low-temperature highly non-exponential kinetics. The transition temperature is at T_k and T₀ < T_k < T_f. In certain low-temperature regimes, a power law behavior at long time emerges. At very low temperatures (lower than trapping transition temperature T < T₀/(46)), the kinetics is an exponential Poissonian process again.

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