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Membrane protein complexes investigated by mass spectormetry

Reference	BB/C510891/1
Principal Investigator / Supervisor	Professor Paula Booth
Co-Investigators / Co-Supervisors	Professor Ian Collinson, Professor Mike Jones
Institution	University of Bristol
Department	Biochemistry
Funding type	Research
Value (£)	25,000
Status	Completed
Type	Research Grant
Start date	01/03/2005
End date	30/11/2005
Duration	9 months

Abstract

Membrane proteins account for about 30 per cent of all cellular proteins coded for by prokaryotic and eukaryotic genomes. These proteins play fundamental roles in biology, acting as signal transducers, transporters as well as being central to ATP production. As a result they are the subject of intensive scientific investigation and are some of the major targets for the pharmaceutical industry. By contrast, there is very little molecular level information on the proteins due, in part, to a lack of appropriate quantitative analytical methods. We intend to extend the application of mass spectrometry in membrane protein research and its unique capability to identify polypeptides in membrane protein complexes with great accuracy. In particular we wish to harness the high-resolution mass detection of Fourier Transform Ion Cyclotron Resonance (FT-ICR), by facilitating the electrospray of membrane proteins with the NanoMate automated sampler. One of the stumbling blocks in mass spectrometry of membrane proteins is finding suitable solvation conditions for protein ionisation, since the hydrophobicity of the proteins limits the use of standard electrospray methods. The NanoMate offers two distinct advantages; it automates the process so that a large number of sample conditions can be screened effectively. In addition, it greatly improves the reproducibility of spraying and sample ionisation over conventional nanospray needles that have inherent variations. We will apply this mass spectrometry approach to three fundamental areas of membrane protein research. Firstly, we will use it to investigate the polypeptide make-up of complex biological membranes, secondly we shall investigate protein, protein interactions involved in membrane translocation and finally we will perform a feasibility study to probe protein protein and protein lipid interactions in oligomeric membrane proteins.

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	Research Equipment Initiative 2004 (RE4) [2004]
Funding Scheme	X – not Funded via a specific Funding Scheme

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