Topological complexity, contact order, and protein folding rates

2002/05/29 by Patrícia F. N. Faísca, P. F. N. Faisca, R. C. Ball
Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #Protein Structure and Dynamics #RNA and protein synthesis mechanisms #cond-mat.soft #q-bio

paper · pdf · doi:10.1063/1.1511509

published as The Journal of Chemical Physics 117, 8587 (2002) · 6 pages, 14 figures

arxiv created 2002/05/29 · openalex publication_date 2002/10/24 · arxiv updated 2009/11/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28

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 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.

Citations

• A Guide to Monte Carlo Simulations in Statistical Physics

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