Award details

Folding and stability of the alpha-helix

Reference	B09794
Principal Investigator / Supervisor	Professor Andrew Doig
Co-Investigators / Co-Supervisors	Professor Gareth Jones
Institution	The University of Manchester
Department	Life Sciences
Funding type	Research
Value (£)	94,640
Status	Completed
Type	Research Grant
Start date	01/10/1998
End date	01/10/2000
Duration	24 months

Abstract

Peptides that form monomeric alpha-helices in aqueous solution provide an excellent system for studying the stability and folding of this protein secondary structure. Using our well established methodology we will measure amino acid preferences for the N-terminal N1, N2 and N3 positions in the helix, His-His and charge-charge side chain interaction energies, the helix preference of alpha-aminoisobutyric acid and phosphoserine and succinate N-cap preferences. We have recently found that helices fold on the millisecond timescale with a transient overshoot in helix content by stopped-flow synchrotron CD. We will follow up this surprising discovery by studying the folding kinetics of helices as a function of temperature and length, investigating the effect of sequence variation on helix folding kinetics and measuring the folding rates of beta-sheets and 3 10-helices.

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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