Conformation-transitional rate in protein folding

Based on the conformation dynamics of macromolecules, the rate of conformational transition is deduced from the nonadiabaticity operator method which can be used to explain the time scale of milliseconds for protein folding. It is proved that (1) the dependence of the transition rate on inertial moment I of the atomic group obeys the I^?2.5 law; (2) its dependence on numbers n of torsional angles participating in the transition obeys the n^1.5 law; and (3) the temperature dependence of the transitional rate shows an abnormal character in the high- temperature region. © 1995 John Wiley & Sons, Inc.