Award details

Systematic analysis of how sequence affects alpha- to-beta structural switching in a straightforward designed peptide system

Reference	B17958/2
Principal Investigator / Supervisor	Professor Dek Woolfson
Co-Investigators / Co-Supervisors
Institution	University of Bristol
Department	Biochemistry
Funding type	Research
Value (£)	31,127
Status	Completed
Type	Research Grant
Start date	17/10/2005
End date	16/04/2006
Duration	6 months

Abstract

We have designed peptides that switch from alpha-helical coiled coils to beta-structured fibrils (amyloid). The work raised several issues. Particularly, how does sequence affect such conformational transitions? Is it passive? i.e., is amyloid formation largely a backbone phenomenon? Or does sequence play a more active role? If so, do certain sequences bias the unfolded state towards nascent beta- structure? Or, are specific side-chain interactions made that assist amyloid formation? These questions will be addressed by combining iterative protein design, peptide synthesis and biophysical characterisations. Our overall objective is to understand the factors that contribute to conformational switching in peptides and proteins. However, the work may also aid the design of peptides for applications in nanobiotechnology.

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

Associated awards:

B17958 Systematic analysis of how sequence affects alpha- to-beta structural switching in a straightforward designed peptide system

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