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The investigation of the conformational interconversion pathway of prion proteins using computer simulation

ReferenceB08012
Principal Investigator / Supervisor Professor Jonathan Essex
Co-Investigators /
Co-Supervisors
Institution University of Southampton
DepartmentSch of Chemistry
Funding typeResearch
Value (£) 91,216
StatusCompleted
TypeResearch Grant
Start date 01/10/1997
End date 01/10/1999
Duration24 months

Abstract

Prion diseases are neurodegenerative disorders that affect both man and other mammals, and include BSE and CJD. Prion illnesses are believed to involve the conformational interconversion of the native prion isoform PrPC to PrPSc. This ultimately results in neuronal cell death. In this proposal the application of molecular dynamics simulations to this problem is described. Simulations of wild type and mutant PrP (121-231) will be performed based on the recent NMR structure. The low frequency vibrations of the protein will be identified, and those involved in the conformational interconversion pathway will be stimulated to drive the conformational transition. Finally, specific ligands will be designed capable of stabilising PrPC.

Summary

unavailable
Committee Closed Committee - Biomolecular Sciences (BMS)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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