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Testing models of helical protein folding via nanosecond temperature jump studies: the B domain of staphylococcal protein A

Reference	BBS/B/04803
Principal Investigator / Supervisor	Professor Sheena Radford
Co-Investigators / Co-Supervisors	Professor David Smith
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	198,386
Status	Completed
Type	Research Grant
Start date	15/07/2004
End date	14/07/2007
Duration	36 months

Abstract

Over the last few years enormous advances in our understanding of the mechanisms of folding have been obtained using both simulation and experiment. Today even the fastest folding events can be monitored experimentally and compared directly with the results from simulation. Here we propose an exciting new project on the B domain of Staphylococcal protein A (BdpA). This small three helix protein has been a paradigm for theoretical studies of folding, yet the rapidity of its folding has precluded experimental verification of these models to date. Using a new laser temperature jump apparatus recently constructed in Leeds capable of measuring rates greater than 1,000,000/s, we propose a series of experiments to determine experimentally how this small helical protein folds. The aim is to test previous models of folding, so that new models can be derived and new theories developed.

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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