Principles of Chaperone-Mediated Protein Folding

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediat...

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Bibliographic Details
Published in:Philosophical transactions of the Royal Society of London. Series B. Biological sciences 1995-04, Vol.348 (1323), p.107-112
Main Author: Hartl, F. Ulrich
Format: Article
Language:English
Subjects:
Aggregation
Catalysts and Chaperones
Chaperonin 60 - chemistry
Chaperonins
Chloroplasts
Cytosol
Heat shock proteins
HSP70 Heat-Shock Proteins - chemistry
Hydrolysis
Mitochondria
Molecular chaperones
Molecular Chaperones - chemistry
Protein Conformation
Protein Folding
Ribosomes
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Summary:The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.
ISSN:0962-8436
1471-2970
DOI:10.1098/rstb.1995.0051