The dissipative dynamics and relaxation behavior of a generic model for hydrophobic collapse (Q2771423)

A generic model of a random polypeptide chain, with discrete torsional degrees of freedom and Hookean springs connecting pairs of hydrophobic residues, reproduces the energy probability distribution of real proteins over a very large range of energies. We show that this system with harmonic interactions, under dissipative dynamics driven by random noise, leads to a distribution of energy states obeying a one-dimensional Ornstein-Uhlenbeck process and giving rise to the so-called Wigner distribution. We find stretched exponential relaxation under Metropolis dynamics at low temperatures with the exponent \(\beta\simeq 1/4\), in agreement with the best experimental results on proteins. The time dependent correlation functions for fluctuations about the native state, computed in the Gaussian approximation for real proteins, have also been found to have the same functional form. Our results indicate that the energy landscape of polypeptide chains exhibits universal features over a very large range of energies and is relatively independent of the specific dynamics.NEWLINENEWLINEFor the entire collection see [Zbl 0959.00018].