Details of Grant 

EPSRC Reference:	EP/D001846/1
Title:	Assembly of a membrane protein pore using single-molecule fluorescence and electrical recording.
Principal Investigator:	Wallace, Professor MI
Other Investigators:	Bayley, Professor H
Researcher Co-Investigators:
Project Partners:
Department:	Oxford Chemistry
Organisation:	University of Oxford
Scheme:	Standard Research (Pre-FEC)
Starts:	04 May 2005	Ends:	03 November 2006	Value (£):	80,533
EPSRC Research Topic Classifications:	Cells Complex fluids & soft solids Lasers & Optics
EPSRC Industrial Sector Classifications:	No relevance to Underpinning Sectors
Related Grants:
Panel History:
Summary on Grant Application Form
Many proteins are present in the membranes of our cells; they constitute approximately 20% of our genome. Their importance is due to their key position, at the interface between the cell and the rest of the world. They are responsible for many important functions within the cell, including signalling and the transport of molecules across the membrane. We would like to develop tools to show how changes in the structure of such molecules are related to changes in their behaviour. This is difficult, as one must have some way of simultaneously measuring how both the structure and the function of a molecule changes.We make measurements on single molecules, and such experiments allow us to see in great detail the underlying behaviour of biomolecules such as membrane proteins. Previous experiments have measured the fluorescence from labelled single membrane proteins. They have also made electrical measurements of the flow of ions through membrane channels. We will develop an instrument capable of making simultaneous single-molecule fluorescence and electrical measurements.We will test the usefulness of such an instrument by studying a simple biological system; the bacterial pore-forming protein, alpha-hemolysin. Understanding how this simple system works will help us figure out how to study more complicated protein interactions on a membrane. alpha-hemolysin is a bacterial protein that forms pores within the membrane of cells. It is composed of 7 identical subunits, and when these 7 subunits combine they form a channel. By simply counting the subunits we will be able to tell if they come together one at a time, or in pairs, or in larger groups. By measuring the electrical current through a pore at the same time as we watch it form, we will be able to understand how these two processes are related. We can determine whether the subunits come together and immediately form a channel capable of conduction, or if there is a significant delay before the pore becomes sufficiently ordered to allow a current to pass.
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Organisation Website:	http://www.ox.ac.uk