Molecular chaperones in protein folding: the art of avoiding sticky situations.
Molecular chaperones are a class of proteins that interact with the non-native conformations of other proteins. The major role of chaperones of the Hsp70 and Hsp60 families is to prevent aggregation of newly synthesized polypeptides and then to mediate their folding to the native state. As a result of functional studies of these proteins, there has been a revision of the long-held view that protein folding in the cell is a spontaneous process.
Hartl
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Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
Hlodan
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Langer
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D000818:Animals; D001426:Bacterial Proteins / Q000502:physiology; D018833:Chaperonins; D005656:Fungal Proteins / Q000502:physiology; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D017510:Protein Folding; D011506:Proteins
D001426:Bacterial Proteins; D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D011506:Proteins; D018833:Chaperonins