Glassy dynamics of protein folding

A coarse-grained model of a random polypeptide chain, with only discrete to rsional degrees of freedom and Hookean springs connecting pairs of hydropho bic residues is shown to display stretched exponential relaxation under Met ropolis dynamics at low temperatures with the exponent beta similar or equa l to 1/4, in agreement with the best experimental results. The time depende nt correlation functions for fluctuations about the native state, computed in the Gaussian approximation for real proteins, have also been found to ha ve the same functional form. Our results indicate that the energy landscape exhibits universal features over a very large rang of energies and is rela tively independent of the specific dynamics.