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Solid-state NMR methods for molecular level studies of amyloid fibrils
Reference
B18705
Principal Investigator / Supervisor
Professor Sheena Radford
Co-Investigators /
Co-Supervisors
Professor David Middleton
,
Professor Peter Stockley
Institution
University of Leeds
Department
Inst of Molecular & Cellular Biology
Funding type
Research
Value (£)
78,704
Status
Completed
Type
Research Grant
Start date
01/08/2003
End date
31/07/2006
Duration
36 months
Abstract
This project proposes to use established solid-state NMR approaches and to develop new methods to probe the molecular architecture of amyloid fibrils formed from human pancreatic amylin and human Beta 2-microglobulin (Beta 2m) The fibrils will be prepared with site selective or uniform isotope labelling and multinuclear (13C, 15N, 2H, 19F) solid-state NMR methods will be used to determine the polypeptide backbone conformation, probe molecular alignment and identify exposed and buried surfaces. This information will provide the first details of the structure of these fibrils and increase our understanding of how these proteins assemble into toxic amyloid species. (Joint with grant 18704).
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
Associated awards:
B18704 Solid-state NMR methods for molecular level studies of amyloid fibrils
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