BBSRC Portfolio Analyser
Award details
Structural biology of the prion protein; function and misfunction
Reference
BS516514
Principal Investigator / Supervisor
Dr John Viles
Co-Investigators /
Co-Supervisors
Professor David Brown
Institution
Queen Mary University of London
Department
Sch of Biological and Chemical Sciences
Funding type
Research
Value (£)
321,468
Status
Completed
Type
Research Grant
Start date
27/05/2002
End date
26/02/2006
Duration
45 months
Abstract
The prion protein (PrP) when misfolded is responsible for CJD in humans and BSE in cattle. PrP is a copper-binding cell surface protein, and the unstructured N-terminal domain cooperatively binds four Cu(II) ions. We aim to determine the structure of PrP in its physiologically relevant copper loaded forms. Folding intermediates of PrP will also be characterised. Using a number of spectroscopic techniques, in particular NMR and CD, we will study recombinant and synthetic fragments of the prion protein. The proposal represents a step towards understanding the function and misfolding process of the prion protein.
Summary
unavailable
Committee
Closed Committee - Agri-food (AF)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Biology of Spongiform Encephalopathies - Phase 5 (BS5) [2001]
Funding Scheme
X – not Funded via a specific Funding Scheme
I accept the
terms and conditions of use
(opens in new window)
export PDF file
back to list
new search