Topological complexity, contact order and protein folding rates

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.

6 pages, 14 figures

Cited by in corpus (5)

• Folding and form: Insights from lattice simulations
• Native geometry and the dynamics of protein folding
• The Go model revisited: Native structure and the geometric coupling between local and long-range contacts
• Folding of small proteins: A matter of geometry?
• Contact Order Dependent Protein Folding Rates: Kinetic Consequences of a Cooperative Interplay Between Favorable Nonlocal Interactions and Local Conformational Preferences