PMID:16100950
| Citation |
Martin, J and Hartl, FU (1993) Protein folding in the cell: molecular chaperones pave the way. Structure 1:161-4 |
|---|---|
| Abstract |
In vitro, many unfolded polypeptides are able to fold to the native state spontaneously, indicating that the amino acid sequence of a protein contains all the information necessary to specify its three-dimensional conformation. It had been assumed that protein folding in vivo also generally occurs in a spontaneous process. This view has changed only recently due to the discovery of a number of proteins, now commonly called 'molecular chaperones', which are essential for cellular protein folding and occur ubiquitously in eubacteria, archaebacteria and in eukaryotic cells. |
| Links | |
| Keywords |
Adenosine Triphosphate/metabolism; Chaperonin 60/metabolism; Escherichia coli Proteins/metabolism; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins/metabolism; Molecular Chaperones/metabolism; Protein Folding |
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