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Title: Contact order revisited: Influence of protein size on the folding rate

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 L2/3, 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{sub 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{sub CO} scales with the protein chain length as L0.70 {+-} 0.07 for the totality of studied single-domain proteins and peptides.
Authors:
; ; ; ; ;
Publication Date:
OSTI Identifier:
827973
Report Number(s):
LBNL--56029
R&D Project: VGTLAA; TRN: US200426%%1033
DOE Contract Number:
AC03-76SF00098
Resource Type:
Journal Article
Resource Relation:
Journal Name: Protein Science; Journal Volume: 12; Other Information: Journal Publication Date: June 2003; PBD: 28 May 2003
Research Org:
Ernest Orlando Lawrence Berkeley National Laboratory, Berkeley, CA (US)
Sponsoring Org:
USDOE Director. Office of Science. Office of Biological and Environmental Research (US)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PEPTIDES; PROTEINS; LAWRENCE BERKELEY LABORATORY PROTEIN FOLDING KINETICS TWO-STATE KINETICS MULTISTATE KINETICS CONTACT ORDER PROTEIN SIZE PROTEIN TOPOLOGY RATE OF FOLDIN