Award details

The characterisation and development of peptides designed to switch structural state

ReferenceB10280
Principal Investigator / Supervisor Professor Dek Woolfson
Co-Investigators /
Co-Supervisors
Institution University of Sussex
DepartmentBiology and Environmental Science
Funding typeResearch
Value (£) 160,823
StatusCompleted
TypeResearch Grant
Start date 01/09/1998
End date 01/09/2001
Duration36 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 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
terms and conditions of use (opens in new window)
export PDF file