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A new approach to the derivation of per-residue thermodynamic parameters for ligand-protein interactions
Reference
B12992
Principal Investigator / Supervisor
Professor Steve Homans
Co-Investigators /
Co-Supervisors
Institution
University of Leeds
Department
Inst of Molecular & Cellular Biology
Funding type
Research
Value (£)
219,980
Status
Completed
Type
Research Grant
Start date
01/04/2000
End date
01/04/2003
Duration
36 months
Abstract
Currently there is much emphasis on high-throughput structural analysis in tandem with gene sequencing. However, if this structural information is to be of value for rational drug design, it is necessary to obtain a deeper understanding of the molecular basis of ligand-protein interactions. We propose to exploit new NMR methodologies by which standard free energies and entropies of binding can be derived on a per-residue basis from NMR relaxation data, thus offering a means by which the thermodynamics of ligand-protein interactions can be characterised at a level of detail that has until now not been possible. We intend to assess these new methodologies by application to a model ligand-protein complex.
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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