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 Nigel Unwin became a staff scientist at the LMB in 1968, after obtaining his Ph.D. from Cambridge University. He left the Laboratory in 1980 to become Professor of Cell Biology at Stanford University, California, and returned in 1988. In 1992 he became Head of the Neurobiology Division, followed by a position as Joint Head of Neurobiology Division from 2003 until 2008.
Nigel has been interested in developing electron microscopical methods and using them to analyse the structures of proteins in membranes. In 1975, together with Richard Henderson, he determined the first structure of an integral membrane protein: bacteriorhodopsin.
More recently, his research has focussed on the structure of the nicotinic acetylcholine receptor - the ligand-gated ion channel at the nerve-muscle synapse - and how it responds to acetycholine released into the synaptic cleft. He obtained an atomic model of this ion channel, in its native membrane setting, in 2005.
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| Our goal is to find out how the acetylcholine receptor works, using electron microscopy to analyse its structure in the closed- and open-channel forms. A comparison of the structure of the closed channel with that of the open channel, obtained by freeze-trapping experiments, yielded a simple mechanistic picture of how binding of acetylcholine opens the gate of the channel. |
Improvement in resolution of the open-channel structure is now being attempted so that the gating mechanism can be described in atomic detail.
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Group Leaders 
