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Investigating the properties of prion proteins using modelling linked to protein characterisation
Reference
BSB11948
Principal Investigator / Supervisor
Dr James Warwicker
Co-Investigators /
Co-Supervisors
Dr James Hope
Institution
The University of Manchester
Department
Life Sciences
Funding type
Research
Value (£)
71,986
Status
Completed
Type
Research Grant
Start date
01/01/2000
End date
14/04/2003
Duration
40 months
Abstract
Solution structures of the PrP-sen folding core and characterisations of recombinant PrP folding and unfolding are available, but definitive links to the mechanism of PrP-sen/PrP-res conversion have not been established. Insolubility (PrP-res) and flexibility (PrP-sen) complicate further structure determination. The proposal links PrP modelling expertise with biophysical studies and in vitro conversions, to probe the folding and interactions of wild- type and mutant PrPs. For example, unfolding of mutants PrPs will test the predicted basis for beta-rich intermediate formation, whilst the conversion reaction will be used with mutants, pH-variation, and under varying conditions, to develop models for PrP- PrP interaction.
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
Biology of Spongiform Encephalopathies - BMS Com (BSEBMS) [1999]
Funding Scheme
X – not Funded via a specific Funding Scheme
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