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Topological complexity, contact order, and protein folding rates

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Faisca, P. F. N. and Ball, R. C.. (2002) Topological complexity, contact order, and protein folding rates. Journal of Chemical Physics, Vol.117 (No.18). pp. 8587-8591. ISSN 0021-9606

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Official URL: http://dx.doi.org/10.1063/1.1511509

Abstract

Monte 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 Ngreater than or equal to54, 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.

Item Type:	Journal Article
Subjects:	Q Science > QC Physics
Divisions:	Faculty of Science > Physics
Library of Congress Subject Headings (LCSH):	Protein folding, Monte Carlo method, Topology, Molecular biology, Thermodynamics, Biophysics
Journal or Publication Title:	Journal of Chemical Physics
Publisher:	American Institute of Physics
ISSN:	0021-9606
Date:	8 November 2002
Volume:	Vol.117
Number:	No.18
Number of Pages:	5
Page Range:	pp. 8587-8591
Identification Number:	10.1063/1.1511509
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Open Access
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URI:	http://wrap.warwick.ac.uk/id/eprint/10415