Structural and mechanistic consequences of polypeptide binding by GroEL.
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-r...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1997
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| _version_ | 1797074648889819136 |
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| author | Coyle, J Jaeger, J Gross, M Robinson, C Radford, SE |
| author_facet | Coyle, J Jaeger, J Gross, M Robinson, C Radford, SE |
| author_sort | Coyle, J |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T23:39:17Z |
| format | Journal article |
| id | oxford-uuid:6ebb36a0-4ab7-4278-86ba-d2bd829e0061 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:39:17Z |
| publishDate | 1997 |
| record_format | dspace |
| spelling | oxford-uuid:6ebb36a0-4ab7-4278-86ba-d2bd829e00612022-03-26T19:26:21ZStructural and mechanistic consequences of polypeptide binding by GroEL.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6ebb36a0-4ab7-4278-86ba-d2bd829e0061EnglishSymplectic Elements at Oxford1997Coyle, JJaeger, JGross, MRobinson, CRadford, SEThe 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. |
| spellingShingle | Coyle, J Jaeger, J Gross, M Robinson, C Radford, SE Structural and mechanistic consequences of polypeptide binding by GroEL. |
| title | Structural and mechanistic consequences of polypeptide binding by GroEL. |
| title_full | Structural and mechanistic consequences of polypeptide binding by GroEL. |
| title_fullStr | Structural and mechanistic consequences of polypeptide binding by GroEL. |
| title_full_unstemmed | Structural and mechanistic consequences of polypeptide binding by GroEL. |
| title_short | Structural and mechanistic consequences of polypeptide binding by GroEL. |
| title_sort | structural and mechanistic consequences of polypeptide binding by groel |
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