| Literature DB >> 12660985 |
Oxana V Galzitskaya1, Sergiy O Garbuzynskiy, Dmitry N Ivankov, Alexei V Finkelstein.
Abstract
We demonstrate that chain length is the main determinant of the folding rate for proteins with the three-state folding kinetics. The logarithm of their folding rate in water (k(f)) strongly anticorrelates with their chain length L (the correlation coefficient being -0.80). At the same time, the chain length has no correlation with the folding rate for two-state folding proteins (the correlation coefficient is -0.07). Another significant difference of these two groups of proteins is a strong anticorrelation between the folding rate and Baker's "relative contact order" for the two-state folders and the complete absence of such correlation for the three-state folders. Copyright 2003 Wiley-Liss, Inc.Entities:
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Year: 2003 PMID: 12660985 DOI: 10.1002/prot.10343
Source DB: PubMed Journal: Proteins ISSN: 0887-3585