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Award details
Physical structure, folding and stability of PrP protein forms
Reference
BBS/E/I/00000606
Principal Investigator / Supervisor
Dr James Hope
Co-Investigators /
Co-Supervisors
Institution
The Pirbright Institute
Department
The Pirbright Institute Department
Funding type
Research
Value (£)
192,526
Status
Completed
Type
Institute Project
Start date
01/04/1997
End date
30/06/1998
Duration
15 months
Abstract
We have made stable, transfected CHO cell lines capable of high-level expression of murine recPrP. Three main forms are produced and have been purified in the presence or absence of detergents and chaotropic agents. ES-MS has confirmed their identity as full-length (23K), N- terminal (9K) and C- terminal (14K) polypeptides and this technique is currently being developed to study the accessibility and fold of these molecules by deuterium exchange, fluorescence and circular dichroism spectrometry.
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
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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