Topological complexity, contact order and protein folding rates

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dc.creatorFaisca, P. F. N.
dc.creatorBall, R. C.
dc.date2002-05-29
dc.date.accessioned2026-07-07T02:45:41Z
dc.date.available2026-07-07T02:45:41Z
dc.descriptionMonte Carlo simulations of protein folding show the emergence of a strong correlation between the relative contact order parameter, CO, and the folding time, t, of two-state folding proteins for longer chains with number of amino acids, N>=54, and higher contact order, CO > 0.17. The correlation is particularly strong for N=80 corresponding to slow and more complex folding kinetics. These results are qualitatively compatible with experimental data where a general trend towards increasing t with CO is indeed observed in a set of proteins with chain length ranging from 41 to 154 amino acids.
dc.description6 pages, 14 figures
dc.identifierhttps://arxiv.org/abs/cond-mat/0205631
dc.identifierhttp://arxiv.org/abs/cond-mat/0205631
dc.identifierThe Journal of Chemical Physics 117, 8587 (2002)
dc.identifierdoi:10.1063/1.1511509
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/19384
dc.subjectSoft Condensed Matter
dc.subjectQuantitative Biology
dc.titleTopological complexity, contact order and protein folding rates
dc.typetext

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