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Solid-state NMR methods for molecular level studies of amyloid fibrils

ReferenceB18705
Principal Investigator / Supervisor Professor Sheena Radford
Co-Investigators /
Co-Supervisors
Professor David Middleton, Professor Peter Stockley
Institution University of Leeds
DepartmentInst of Molecular & Cellular Biology
Funding typeResearch
Value (£) 78,704
StatusCompleted
TypeResearch Grant
Start date 01/08/2003
End date 31/07/2006
Duration36 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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