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Mechanical unfolding of proteins monitored by simultaneous laser induced fluorescence spectroscopy

Reference	9912375
Principal Investigator / Supervisor	Professor Sheena Radford
Co-Investigators / Co-Supervisors
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	126,432
Status	Completed
Type	Research Grant
Start date	01/10/1999
End date	01/10/2001
Duration	24 months

Abstract

It has recently been demonstrated that proteins can be unfolded mechanically using at atomic force microscope (AFM). Most importantly, individual protein molecules can be unfolded and refolded using AFM, providing a unique opportunity to study the mechanism of protein folding of a single molecule. A draw-back to this approach, however, is that structural information about the events occurring during folding cannot be obtained using the AFM alone. Here we propose to build a new instrument capable of correlating forces measured during mechanical unfolding with structural changes detected by single molecule fluorescence. The proposal is thus ideally suited to ROPA in that it is pump- priming (building a new experiment), speculative (attempting single molecule trytophan fluorescence) and will prove the concept of combined AFM:fluorescence experiments.

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	ROPA 1999 (ROPA1999) [1999]
Funding Scheme	X – not Funded via a specific Funding Scheme

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