Received January 27, 2010; Revision received February 24, 2010
Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state kinetics from the size range 101-151 a.a. fold faster than those from the size range 50-100 a.a. Moreover, it turns out unexpectedly that usually in the group of structural homologs from the size range 50-100 a.a., proteins with multi-state kinetics fold faster than those with two-state kinetics. The protein folding for six proteins with a ferredoxin-like fold and with a similar size has been modeled using Monte Carlo simulations and dynamic programming. Good correlation between experimental folding rates, some structural parameters, and the number of Monte Carlo steps has been obtained. It is shown that a protein with multi-state kinetics actually folds three times faster than its structural homologs.
KEY WORDS: protein folding, intermediates of folding, two-state transition, folding nucleus, folding rates