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Design folding and co-operative interactions in beta-sheet peptides
Reference
B13465
Principal Investigator / Supervisor
Professor Mark Searle
Co-Investigators /
Co-Supervisors
Institution
University of Nottingham
Department
Sch of Chemistry
Funding type
Research
Value (£)
167,596
Status
Completed
Type
Research Grant
Start date
01/10/2000
End date
07/01/2004
Duration
39 months
Abstract
The importance of a beta-sheet structure in the formation of amyloid fibrils, and their role in a variety of pathological disease states (Alzheimers and BSE) suggests that model beta-sheet peptides may provide insight into the molecular basis and sequence dependence of sheet formation, the origin of their stability and the importance of co-operative interactions in their propagation. We investigate these phenomena using rationally designed two and three-stranded beta-sheet peptides using a variety of spectroscopic probes and theoretical methods to simulate folding. We focus on a quantitative description of stability and co-operative interactions both parallel and perpendicular to the strand direction using model systems already established in our group, and expand the design strategy to incorporate arrays of ionic interactions in addition to conventional hydrophobic motifs.
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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