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Protein Folding in the Cell: The Role of Molecular Chaperones Hsp70 and Hsp60

Protein Folding in the Cell: The Role of Molecular Chaperones Hsp70 and Hsp60 293 1056-8700/92/0610-0293$02.00 HARTL, MARTIN & NEUPERT PERSPECTIVES AND OVERVIEW The fundamental discovery that the amino acid sequence of a protein contains the full information specifying its native, three-dimensional con­ formation marked the beginning of an era of active biophysical research on the pathways and thermodynamics of protein folding (3). Many purified proteins when denatured to random coil-like structures can refold spon­ taneously in vitro. This action is driven by small differences in the Gibbs free energy between the unfolded and native states (33, 38, 92, 97). Conse­ quently, researchers assumed that in vivo folding (acquisition of tertiary structure) and assembly (acquisition of quarternary structure) of newly synthesized polypeptides also occur by an essentially spontaneous process without the help of additional components. Over recent years, however, several proteinaceous components have been discovered that directly influence the processes by which newly made proteins attain their final conformation within the cell. With the exception of the enzymes protein disulfide isomerase and peptidyl prolyl isomerase, which catalyze specific reactions that can be rate limiting for folding (reviewed in 53, 62, 63, 64), these components have been classified as molecular chaperones (46, 48, 49) or polypeptide-chain binding proteins ( 1 68). They occur http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Biophysics Annual Reviews

Protein Folding in the Cell: The Role of Molecular Chaperones Hsp70 and Hsp60

Hartl, F U; Martin, J; Neupert, W
Annual Review of Biophysics , Volume 21 (1) – Jun 1, 1992
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References (34)

Publisher
Annual Reviews
Copyright
Copyright 1992 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
1936-122X
eISSN
1936-1238
DOI
10.1146/annurev.bb.21.060192.001453
pmid
1525471
Publisher site
See Article on Publisher Site

Abstract

293 1056-8700/92/0610-0293$02.00 HARTL, MARTIN & NEUPERT PERSPECTIVES AND OVERVIEW The fundamental discovery that the amino acid sequence of a protein contains the full information specifying its native, three-dimensional con­ formation marked the beginning of an era of active biophysical research on the pathways and thermodynamics of protein folding (3). Many purified proteins when denatured to random coil-like structures can refold spon­ taneously in vitro. This action is driven by small differences in the Gibbs free energy between the unfolded and native states (33, 38, 92, 97). Conse­ quently, researchers assumed that in vivo folding (acquisition of tertiary structure) and assembly (acquisition of quarternary structure) of newly synthesized polypeptides also occur by an essentially spontaneous process without the help of additional components. Over recent years, however, several proteinaceous components have been discovered that directly influence the processes by which newly made proteins attain their final conformation within the cell. With the exception of the enzymes protein disulfide isomerase and peptidyl prolyl isomerase, which catalyze specific reactions that can be rate limiting for folding (reviewed in 53, 62, 63, 64), these components have been classified as molecular chaperones (46, 48, 49) or polypeptide-chain binding proteins ( 1 68). They occur

Journal

Annual Review of Biophysics – Annual Reviews

Published: Jun 1, 1992

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