Award details

Structure and function of PrP

Reference	BBS/E/I/00000877
Principal Investigator / Supervisor	Dr Andrew Gill
Co-Investigators / Co-Supervisors
Institution	The Pirbright Institute
Department	The Pirbright Institute Department
Funding type	Research
Value (£)	465,894
Status	Completed
Type	Institute Project
Start date	01/08/2001
End date	31/03/2007
Duration	68 months

Abstract

The conversion of PrPC to PrPSc appears to involve a conformational transition in the protein. Various post-translational modifications have been detected in both normal and abnormal forms of the prion protein and it is possible that variations in, or alterations to, the primary structure of PrPC could facilitate the conversion process, could be important in determining strain characteristics or could have a role in the normal structure and function of PrP. This project is aimed at characterising the primary structures of different forms of the prion protein to assess the individual structures and extents of modifications, primarily by means of mass spectrometry. It is envisaged that novel modifications, or novel variations of previously identified modifications, may be used for disease or strain diagnosis. By use of recombinant proteins and synthetic peptides, the effect that individual modifications may have on the structure and function of PrP will be probed. Such investigations will make use of biophysical techniques such as circular dichroism and fluorescence spectrometry and, ideally, will compliment results of cell biological experiments using modified prion proteins. Proteins will be labelled to allow their specific detection in cell cultures and other systems.

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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