NDLI: Protein folding: how the mechanism of GroEL action is defined by kinetics.

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Protein folding: how the mechanism of GroEL action is defined by kinetics.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Frieden, C. Clark, A. C.
Description	Author Affiliation: Frieden C ( Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA. frieden@biochem.wustl.edu);
Abstract	We propose a mechanism for the role of the bacterial chaperonin GroEL in folding proteins. The principal assumptions of the mechanism are (i) that many unfolded proteins bind to GroEL because GroEL preferentially binds small unstructured regions of the substrate protein, (ii) that substrate protein within the cavity of GroEL folds by the same kinetic mechanism and rate processes as in bulk solution, (iii) that stable or transient complexes with GroEL during the folding process are defined by a kinetic partitioning between formation and dissociation of the complex and the rate of folding and unfolding of the protein, and (iv) that dissociation from the complex in early stages of folding may lead to aggregation but dissociation at a late stage leads to correct folding. The experimental conditions for refolding may play a role in defining the function of GroEL in the folding pathway. We propose that the role of GroES and MgATP, either binding or hydrolysis, is to regulate the association and dissociation processes rather than affecting the rate of folding.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chaperonin 60 Metabolism Protein Folding Proteins Chemistry Adenosine Triphosphate Animals Chaperonin 10 Kinetics Mice Models, Chemical Protein Binding Tetrahydrofolate Dehydrogenase Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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