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The characterisation and development of peptides designed to switch structural state
Reference
B10280
Principal Investigator / Supervisor
Professor Dek Woolfson
Co-Investigators /
Co-Supervisors
Institution
University of Sussex
Department
Biology and Environmental Science
Funding type
Research
Value (£)
160,823
Status
Completed
Type
Research Grant
Start date
01/09/1998
End date
01/09/2001
Duration
36 months
Abstract
Structural switching in proteins is implicated in viral infection, Alzheimer's dementia and prion diseases. Here, we describe two peptides that are designed to switch structural state in response to changes in solution conditions. Each peptide carries a sequence motif for a parallel coiled-coil dimer in combination with another for either a beta-hairpin, or an antiparallel coiled coil. Synthetic peptides will be made and initially constrained in starting conformations (beta-hairpin, or antiparallel coiled coil), using intramolecular disulphide bonds. The transition to the switched conformation (coiled-coil dimer) will be triggered by disulphide reduction. The designs will be characterised by CD, NMR and analytical ultracentrifugation. This study will test our understanding of sequence-structure relationships and provide models for protein-structure switches.
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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