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Structural and functional details of membrane transport proteins from solid state NMR
Reference
B14769
Principal Investigator / Supervisor
Professor Anthony Watts
Co-Investigators /
Co-Supervisors
Dr Paul Spooner
Institution
University of Oxford
Department
Biochemistry
Funding type
Research
Value (£)
230,432
Status
Completed
Type
Research Grant
Start date
01/01/2001
End date
31/12/2003
Duration
36 months
Abstract
Our recent advances in solid state NMR methodology will be extended to exploit interactions between specifically bound ligands and binding environment to define residues involved at the sites of action of fully functional, membrane embedded solute transporters. Uniquely, these proteins are expressed at amplified levels (20-60% of total protein) in bacterial membranes and can be uniformly or specifically labelled with non-perturbing, NMR visible (13C, 15N) isotopes. The information will compliment recent 2D crystallographic information (at >6 Angstrom) on one member of this class of protein to help develop molecular mechanisms for exchange dynamics and binding mechanisms (electrostatic/H-bond details) for which NMR is well suited.
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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