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Protein engineering and NMR structure of solubilised domains of globular proteins
Reference
MOL04551
Principal Investigator / Supervisor
Professor Richard Perham
Co-Investigators /
Co-Supervisors
Institution
University of Cambridge
Department
Biochemistry
Funding type
Research
Value (£)
139,096
Status
Completed
Type
Research Grant
Start date
14/08/1995
End date
14/08/1998
Duration
36 months
Abstract
The structures of novel, solubilised forms of the interface domain (responsible for the dimerisation) from the homologous flavoprotein disulphide oxidoreductases, glutathione reductase and dihydrolipoyl dehydrogenase, will be determined by means of 3D and 4D NMR spectroscopy These will be compared with the structures of the same domains, determined elsewhere by X-ray crystallography. The results will throw important new light on the processes of molecular recognition that underlie assembly of the dimeric enzymes, on the relationship of buried surface area to protein stability, and on the assembly of the 2-oxo acid dehydrogenase complex of which dihydrolipoyl dehydrogenase is part.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Molecules (Ropa) (MOL) [1994]
Funding Scheme
X – not Funded via a specific Funding Scheme
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