Contact order revisited: influence of protein size on the folding rate

TitleContact order revisited: influence of protein size on the folding rate
Publication TypeJournal Article
Year of Publication2003
AuthorsIvankov, D. N., Garbuzynskiy S. O., Alm E., Plaxco K. W., Baker D., & Finkelstein A. V.
JournalProtein science
Volume12
Issue9
Pagination2057-62
Date Published2003 Sep
ISSN0961-8368
KeywordsAnimals, Collaborative Publication, Kinetics, Models, Chemical, Models, Statistical, Peptides, Protein Folding, Protein Structure, Secondary, Proteins, Proteomics, Thermodynamics, Time Factors, Water
Abstract

Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L(2/3), and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO x L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs_CO scales with the protein chain length as L(0.70 +/- 0.07) for the totality of studied single-domain proteins and peptides.

Alternate JournalProtein Sci.
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