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Chemically synthesised ubiquitin analogues as probes of protein folding dynamics and structure

ReferenceB06742
Principal Investigator / Supervisor Professor Robert Ramage
Co-Investigators /
Co-Supervisors
Professor Paul Barlow, Professor D Young
Institution University of Edinburgh
DepartmentSch of Chemistry
Funding typeResearch
Value (£) 183,079
StatusCompleted
TypeResearch Grant
Start date 25/10/1996
End date 30/06/1999
Duration32 months

Abstract

The folding, stability, structure, dynamics and functional properties of chemically synthesised ubiquitin analogues containing unnatural branched, straight-chain and fluorinated alpha-amino acids will be characterised by 600 MHz NMR, X-ray crystallography and other relevant physical techniques. The results will contribute to efforts to understand protein folding at the level of atomic interactions.

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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