Dissipative Dynamics and the Statistics of Energy States of a Hookean Model for Protein Folding

Details Dissipative Dynamics and the Statistics of Energy States of a Hookean Model for Protein Folding Dissipative Dynamics and the Statistics of Energy States of a Hookean Model for Protein Folding

1999-09-23

arxiv.org/abs/cond-mat/9909350v2

J. Stat. Phys. 100 (1/2), 405-422 (2000).

Physics

Condensed Matter

Soft Condensed Matter

RevTeX, 24 pages, including 8 figures

Scientific paper

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 modified one-dimensional Ornstein-Uhlenbeck process and giving rise to the so called Wigner distribution. A tunably fine- or coarse-grained sampling of the energy landscape yields a family of distributions for the energies and energy spacings.

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