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Structural and mechanistic consequences of polypeptide binding by GroEL.

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...

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
Journal:
Folding and design
Volume:
2
Issue:
6
Pages:
R93-104
Publication date:
1997-01-01
DOI:
ISSN:
1359-0278
Source identifiers:
60305
Language:
English
Keywords:
Pubs id:
pubs:60305
UUID:
uuid:6ebb36a0-4ab7-4278-86ba-d2bd829e0061
Local pid:
pubs:60305
Deposit date:
2013-02-20

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