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Structural variations of prion proteins
Reference
BBS/E/A/00001663
Principal Investigator / Supervisor
Dr Andrew Gill
Co-Investigators /
Co-Supervisors
Institution
The Roslin Institute
Department
The Roslin Institute Department
Funding type
Research
Value (£)
115,849
Status
Completed
Type
Institute Project
Start date
01/04/2007
End date
31/03/2010
Duration
36 months
Abstract
This project aims to use various techniques to probe differences in prion protein properties that may impinge on the ability of these proteins to convert to pathogenic isoforms. It also aims to characterise those sites not typically associated with susceptibility, since they are not naturally polymorphic. The project objectives are to define structural variability in prion protein mutants, to characterise the effect of mutations of PrP conversion and to map the important sites for PrP conversion based on mutation to non-naturally-occurring amino acids.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
Animal Health, Structural Biology, TSEs (transmissible spongiform encephalopathies)
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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