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The catalytic mechanism of aspartic proteinases: locating the active site protons by neutron laue diffraction

Reference	B10069
Principal Investigator / Supervisor	Professor Jon Cooper
Co-Investigators / Co-Supervisors
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	94,156
Status	Completed
Type	Research Grant
Start date	01/11/1998
End date	01/11/2000
Duration	24 months

Abstract

The proposed work involves determination of the proton positions at the catalytic centre of an aspartic proteinase using high resolution neutron diffraction data. Until now, no aspartic proteinase has been subjected to a neutron study due to the limited size of the crystals. However due to recent technical breakthroughs at ILL (Grenoble), we have succeeded in collecting neutron Laue data to 2.2 angstroms on a complex of endothiapepsin with a transition state analogue (with Dr D. Myles, ILL). Suitable crystals of other complexes as well as the native enzyme await data collection. In line with work on serine proteinases where neutron diffraction has provided some of the most definitive data on the catalytic mechanism, we expect that our work will have a greater impact on understanding of the aspartic proteinase enzymes where mechanistic studies have hitherto been much less conclusive.

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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