- Abstract:
-
The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of proteins constitutes one of the most fascinating molecular recognition events in protein chemistry. Recent structural studies have revealed a possible model for substrate binding by GroEL and a high-resolution image of the GroEL-GroES folding machinery has provided important new insights into our understanding of the mechanism of action of this chaperonin. Studies with a variety of model substr...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/S1359-0278(97)00046-1
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- Journal:
- Folding and design
- Volume:
- 2
- Issue:
- 6
- Pages:
- R93-104
- Publication date:
- 1997-01-05
- DOI:
- ISSN:
-
1359-0278
- URN:
-
uuid:6ebb36a0-4ab7-4278-86ba-d2bd829e0061
- Source identifiers:
-
60305
- Local pid:
- pubs:60305
- Copyright date:
- 1997
Journal article
Structural and mechanistic consequences of polypeptide binding by GroEL.
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