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(A) Direct visualisation of elasticity in single titin molecules

Reference	JE412942
Principal Investigator / Supervisor	Professor John Trinick
Co-Investigators / Co-Supervisors
Institution	University of Leeds
Department	Institute of Membrane & Systems Biology
Funding type	Research
Value (£)	16,064
Status	Completed
Type	Research Grant
Start date	01/03/2000
End date	01/09/2000
Duration	6 months

Abstract

The goal is to understand the molecular mechanism of elasticity in the giant (3 MDa) muscle protein titin. We proposed that this mechanism involves unfolding of the polypeptide and have previously demonstrated this in different parts of the molecule using optical tweezers and electron microscopy. We are now exploring chain unfolding in greater detail by pulling single titin molecules by atomic force microscopy (AFM). The apparatus requested here will allow us to mount the AFM on an inverted light microscope. Images of titin molecules labelled with fluorescent dyes will then be recorded on the camera requested during extensions imposed by AFM. This will allow recording and exploration of the several different phases of elasticity predicted for different parts of the molecule. These mechanisms are directly relevant to the elasticity of muscle and to protein folding in general. The coupling of atomic force spectroscopy to fluorescence microscopy is a novel and generally applicable method.

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	Joint Equipment Initiative 1999 (JE4) [1999]
Funding Scheme	X – not Funded via a specific Funding Scheme

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