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Characterisation of hybrid GroEL molecular chaperones
Reference
C05942
Principal Investigator / Supervisor
Professor Peter Lund
Co-Investigators /
Co-Supervisors
Institution
University of Birmingham
Department
Sch of Biosciences
Funding type
Research
Value (£)
166,238
Status
Completed
Type
Research Grant
Start date
07/10/1996
End date
06/10/1999
Duration
36 months
Abstract
The discovery of molecular chaperones has changed our understanding of how proteins fold in vivo. The GroEL molecular chaperone consists of two rings of seven protomers each. The protomers show positive cooperativity, and the two rings show negativity cooperativity with respect to ATP binding and hydrolysis; thus these properties are usually fundamental to models of GroEL mechanism. However, we have recently made hybrid GroEL proteins which are active both in vivo and in vitro as single heptameric rings and show no cooperativity. This proposal is to study such structures in more detail. This should provide new insights into the reaction mechanism of the GroEL family of molecular chaperones.
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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