[Magazine] Scientific American. Vol. 269. No 5

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Extra resources for [Magazine] Scientific American. Vol. 269. No 5

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We needed more data in order to test that idea, but in the interim we had to cope with another nagging problem. Could we be sure that receptor molecules contained an ion channel, not solely the site that bound acetylcholine? In 1974 my co-worker Gerald L. Ha- SCIENTIFIC AMERICAN November 1993 Anatomy of the Acetylcholine Receptor M ajor structural features of the acetylcholine receptor have begun to yield to scrutiny. Its five subunits (inset in top panel ), which can be depicted schematically as cylinders (top, center ), are each formed from a protein that has folded in on itself (detail at top right ).

The muscle receptor turned out to differ little from those of electrocytes. T hese studies put workers in an excellent position to ascertain something about the architecture of the folded subunits and how they might Þt together. In trying to predict the structure of a folded protein, scientists often scan the linear amino acid sequence for stretches that are rich in either hydrophilic or hydrophobic amino acids. Hydrophilic substances are attracted to water, such as that in cytoplasm or in the ßuids that bathe cells; hydrophobic, or water-hating, substances prefer to associate with other hydrophobic entities, such as the lipids that form cell membranes.

Translated by Laurence Garey. Pantheon Books, 1985. FUNCTIONAL ARCHITECTURE AND DYNAMICS OF THE NICOTINIC ACETYLCHOLINE RECEPTOR: AN ALLOSTERIC LIGAND-GATED ION CHANNEL. J. P. Changeux in FIDIA Research Foundation Neuroscience Award Lectures, Vol. 4. Raven Press, 1990. EXPLORATIONS OF THE NICOTINIC ACETYLCHOLINE RECEPTOR. A. Karlin in Harvey Lectures: 1989Ð1990, Vol. 85, 62 pages 71Ð107; 1991. THE FUNCTIONAL ARCHITECTURE OF THE ACETYLCHOLINE NICOTINIC RECEPTOR EXPLORED BY AFFINITY LABELLING AND SITEDIRECTED MUTAGENESIS.

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