BBSRC Portfolio Analyser
Award details
Modelling secondary interactions in the active site of carbonic anhydrase
Reference
B08597
Principal Investigator / Supervisor
Professor Paul Walton
Co-Investigators /
Co-Supervisors
Institution
University of York
Department
Chemistry
Funding type
Research
Value (£)
163,180
Status
Completed
Type
Research Grant
Start date
05/01/1998
End date
05/01/2001
Duration
36 months
Abstract
The work aims to prepare small molecule model complexes of the active site of the metalloenzyme, carbonic anhydrase. The models are novel insofar as they aim to model the whole of the active site - including the amino acids remote from the primary metal coordination sphere. In this way, the weak intermolecular forces (or secondary interactions), which are so important in the high catalytic efficiency of the enzyme, can be studied in synthetic complexes. The models are based on ligands derived from cis- 1,3,5-triaminocyclohexane.
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
I accept the
terms and conditions of use
(opens in new window)
export PDF file
back to list
new search