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Atomic resolution X-ray neutron and NMR studies of aspartic proteinase structure and function

Reference	B14709
Principal Investigator / Supervisor	Professor Jon Cooper
Co-Investigators / Co-Supervisors	Professor Matthew Crump, Professor Stephen Wood
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	195,048
Status	Completed
Type	Research Grant
Start date	01/05/2001
End date	30/09/2004
Duration	41 months

Abstract

Aspartic proteinases are involved in numerous important biological processes and inhibitors have a proven record in the treatment of AIDS. We propose to analyse the fungal aspartic proteinase endothiapepsin as a model system for detailed studies of the mechanism and dynamics. Recently, we have used neutron and atomic resolution X-ray diffraction which have yielded much information on the proton locations at the catalytic centre and we have evidence for a novel mode of inhibition of the enzyme. In addition, we have obtained from crystallography and NMR the first evidence that catalysis involves low-barrier hydrogen bonds. We now propose to build on these studies by expressing isotopically labelled enzyme for further NMR and neutron studies of the aspartic proteinase mechanism and the role of conformational flexibility.

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	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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