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Structure of membrane transport proteins determined by solid-state NMR: synthesis of labelled amino acids and ligands
Reference
B10959
Principal Investigator / Supervisor
Professor Peter Henderson
Co-Investigators /
Co-Supervisors
Dr R Herbert
,
Professor Chris Willis
Institution
University of Leeds
Department
Inst of Molecular & Cellular Biology
Funding type
Research
Value (£)
190,256
Status
Completed
Type
Research Grant
Start date
01/05/1999
End date
01/07/2002
Duration
38 months
Abstract
We aim to elucidate the 3-D structures of the ligand-binding site complexes of membrane transport proteins by exploiting leading-edge solid state magic angle spin NMR technologies. Resources are requested to synthesise chemically homochiral L-alpha-amino acids (in 500mg amounts) and ligands, namely beta-glucosides (membrane transport protein: Bg1), glucuronides (GusB), and nucleotides (NupC), labelled with 13C/15N/19F in specific positions. The labelled amino acids will be incorporated into the individual proteins. Precise distances between labels in amino-acid residues and bound ligand will then be determined by solid-state NMR, so defining 3D structure.
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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