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

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dc.creatorTuzel, Erkan
dc.creatorErzan, Ayse
dc.date1999-09-23
dc.date1999-12-21
dc.date.accessioned2026-07-07T03:14:38Z
dc.date.available2026-07-07T03:14:38Z
dc.descriptionA 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.
dc.descriptionRevTeX, 24 pages, including 8 figures
dc.identifierhttps://arxiv.org/abs/cond-mat/9909350
dc.identifierhttp://arxiv.org/abs/cond-mat/9909350
dc.identifierJ. Stat. Phys. 100 (1/2), 405-422 (2000).
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/29744
dc.subjectSoft Condensed Matter
dc.subjectStatistical Mechanics
dc.subjectBiomolecules
dc.titleDissipative Dynamics and the Statistics of Energy States of a Hookean Model for Protein Folding
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