NDLI: Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.

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Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fersht, A. R.
Description	Author Affiliation: Fersht AR ( Department of Chemistry, University of Cambridge, United Kingdom.);
Abstract	Small, single-module proteins that fold in a single cooperative step may be paradigms for understanding early events in protein-folding pathways generally. Recent experimental studies of the 64-residue chymotrypsin inhibitor 2 (CI2) support a nucleation mechanism for folding, as do some computer stimulations. CI2 has a nucleation site that develops only in the transition state for folding. The nucleus is composed of a set of adjacent residues (an alpha-helix), stabilized by long-range interactions that are formed as the rest of the protein collapses around it. A simple analysis of the optimization of the rate of protein folding predicts that rates are highest when the denatured state has little residual structure under physiological conditions and no intermediates accumulate. This implies that any potential nucleation site that is composed mainly of adjacent residues should be just weakly populated in the denatured state and become structured only in a high-energy intermediate or transition state when it is stabilized by interactions elsewhere in the protein. Hierarchical mechanisms of folding in which stable elements of structure accrete are unfavorable. The nucleation-condensation mechanism of CI2 fulfills the criteria for fast folding. On the other hand, stable intermediates do form in the folding of more complex proteins, and this may be an unavoidable consequence of increasing size and nucleation at more than one site.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Peptides Chemistry Protein Folding Serine Proteinase Inhibitors Chymotrypsin Antagonists & Inhibitors Computer Simulation Hordeum Enzymology Kinetics Plant Proteins Protein Denaturation Protein Structure, Tertiary Thermodynamics Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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