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Proceedings Paper

Use of fluorescence spectroscopy to elucidate structural features of the nicotinic acetylcholine receptor
Author(s): David Allen Johnson; C. Fernando Valenzuela
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Paper Abstract

The authors review three examples of how fluorescence spectroscopic techniques have been employed to elucidate structural features of the nicotinic acetylcholine receptor from the electric organ of Torpedo californica. The instrumentation and most relevant fluorescence methods utilized for these studies are briefly discussed. The examples reviewed are as follows: (1) the measurement of the average distance between the two acetylcholine binding sites on the receptor and the noncompetitive inhibitor binding site in the central ion channel, (2) the measurement of distance between fluorescently labeled snake (alpha) -toxins bound to the same membrane-associated receptor oligomer and bound to the adjacent receptor oligomers, and (3) the relative orientation of snake (alpha) -toxin with respect to the central ion channel and the plane of the lipid membrane into which the receptor is embedded.

Paper Details

Date Published: 1 June 1991
PDF: 9 pages
Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991); doi: 10.1117/12.44210
Show Author Affiliations
David Allen Johnson, Univ. of California/Riverside (United States)
C. Fernando Valenzuela, Univ. of California/Riverside (United States)

Published in SPIE Proceedings Vol. 1432:
Biomolecular Spectroscopy II
Robert R. Birge; Laurence A. Nafie, Editor(s)

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