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Assessment of the extent to which 3D structure predicts variation in chemical behaviour in an enzyme family

ReferenceB01947
Principal Investigator / Supervisor Professor K Brocklehurst
Co-Investigators /
Co-Supervisors
Institution Queen Mary University of London
DepartmentSch of Biological and Chemical Sciences
Funding typeResearch
Value (£) 151,556
StatusCompleted
TypeResearch Grant
Start date 01/02/1995
End date 15/04/1998
Duration38 months

Abstract

(i) To contribute to understanding the ways in which binding interactions and remote ionisations determine catalytic site behaviour by stopped-flow kinetic analysis using systematic structural variation in a uniquely available series of time-dependent inhibitors and analogous substrates (ii) to assess the extent to which 3D-structures of the enzymes predict variation in chemical behaviour in an enzyme family using selected cysteine proteinases as a testbed (iii) to delineate the effects of specific binding interactions on the separate entropic and enthalpic contributions to reactivity.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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