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An ultra-violet resonance Raman probe of sub-millisecond protein folding

Reference	E16849
Principal Investigator / Supervisor	Professor David Smith
Co-Investigators / Co-Supervisors	Professor Sheena Radford
Institution	University of Leeds
Department	Physics and Astronomy
Funding type	Research
Value (£)	129,864
Status	Completed
Type	Research Grant
Start date	15/07/2002
End date	15/07/2004
Duration	24 months

Abstract

Many proteins fold through intermediates that are populated within the 2-3 ms dead time of conventional stopped flow instruments. As a result, the nature of key events in the folding pathway that occur on faster time scales cannot be studied. Smith and Radford have collaborated over the past few years to develop new technologies necessary to address important questions in post-genome structural biology. As part of this collaboration we have developed a rapid mixing experiment capable of measuring protein folding with a dead time of about 150 microsecs. Although fluorescence intensity that is used in this experiment provides a good probe of the kinetics of folding it does not provide detailed structural information vital to our understanding of folding pathways and intermediate states. Here we propose a two year feasibility study to demonstrate that ultra-violet resonance Raman spectroscopy can be combined with sub-millisecond mixing to provide uniquely detailed secondary and tertiary information about protein conformational dynamics with high temporal resolution.

Summary

unavailable

Committee	Closed Committee - Engineering & Biological Systems (EBS)
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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