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Structural studies of beta 2 microglobulin amyloid fibrils by cryo-electron microscopy and image processing
Reference
B18659
Principal Investigator / Supervisor
Professor Helen Saibil
Co-Investigators /
Co-Supervisors
Professor Sheena Radford
Institution
Birkbeck College
Department
Biological Sciences
Funding type
Research
Value (£)
223,208
Status
Completed
Type
Research Grant
Start date
01/09/2003
End date
31/08/2006
Duration
36 months
Abstract
Amyloid has been found to be a generic state of polypeptide chains. Despite its importance in both structural biology and in disease, little is known about the 3D structure of amyloid. Here we propose to determine the structure of amyloid fibrils assembled from a well- characterised intermediate of Beta 2 microglobulin. At Birkbeck, we have developed a combination of helical and single particle cryo electron microscopy to study the structure of amyloid fibrils. The Leeds group have characterised the monomeric amyloidgenic intermediate to Beta 2 microglobulin and can precisely control fibril assembly. This new collaboration will provide a powerful approach to fill the information gap between the cross-beta fold and 3D conformation in amyloid.
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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