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NCMH stage V: molecular crowding and thermodynamic non-ideality prediction for macromolecule-ligand interactions
Reference
B18660
Principal Investigator / Supervisor
Professor Stephen Harding
Co-Investigators /
Co-Supervisors
Professor John King
Institution
University of Nottingham
Department
Sch of Biosciences
Funding type
Research
Value (£)
261,868
Status
Completed
Type
Research Grant
Start date
02/06/2003
End date
01/06/2006
Duration
36 months
Abstract
75 per cent: We address significant non-ideality crowding and hydration problems in solution biophysics, concerning macromolecule-macromolecules and macromolecule-small ligand interactions. Facilitates full characterisation of one specific and important example in the field of metabolic biochemistry: the phosphorylase b dimer (inactive) - tetramer (active) equilibrium. Rallison-Harding theory is then applied to a series of NON-self associating macromolecular systems of known structure to pinpoint molecular hydration delta for proteins and glycoproteins: involves thorough determination of the virial coefficient and charge, application of the J. Thornton ELLIPSE algorithm to the crystal structure and our COVOL algorithm. 25 per cent: NCMH Facility for UK users.
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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