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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 substrates reveal that the binding of substrate proteins to GroEL is not just a passive event, but can result in significant changes in the structure and stability of the bound polypeptide. The potential impact of this on the mechanism of chaperonin-assisted folding is not fully understood, but provides exciting scope for further experiment.

Original publication

DOI

10.1016/S1359-0278(97)00046-1

Type

Journal article

Journal

Fold Des

Publication Date

1997

Volume

2

Pages

R93 - 104

Keywords

Amino Acid Sequence, Chaperonin 60, Models, Molecular, Molecular Sequence Data, Peptides, Protein Binding, Protein Conformation, Protein Folding, Structure-Activity Relationship