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Characterisation of active single ring forms of the essential molecular chaperone GroEL
Reference
C16679
Principal Investigator / Supervisor
Professor Peter Lund
Co-Investigators /
Co-Supervisors
Institution
University of Birmingham
Department
Sch of Biosciences
Funding type
Research
Value (£)
242,092
Status
Completed
Type
Research Grant
Start date
01/08/2002
End date
01/08/2005
Duration
36 months
Abstract
The molecular chaperone GroEL assists the folding of proteins under normal and stressed conditions, by encapsidating substrate proteins in a cavity capped by the cofactor GroES. It has two rings, each composed of seven identical sub-units, with allosteric interactions between sub-units in the same ring and between rings. The double ring has been thought to be essential, We have recently isolated several mutants of GroEL which form single rings and yet which are still fully active in vivo. This project will characterise in detail the in vivo and in vitro properties of these mutants, and use this information to extend our understanding of how the mechanism of this essential protein is determined by its structure.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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