Award details

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

Reference	B18704
Principal Investigator / Supervisor	Professor David Middleton
Co-Investigators / Co-Supervisors	Professor Sheena Radford, Professor Peter Stockley
Institution	The University of Manchester
Department	Life Sciences
Funding type	Research
Value (£)	151,344
Status	Completed
Type	Research Grant
Start date	25/08/2003
End date	24/11/2006
Duration	39 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 18705).

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:

B18705 Solid-state NMR methods for molecular level studies of amyloid fibrils

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