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Fluorescence nicotinic acetylcholine receptor

S. L. Pearce and E. Hawrot, Intrinsic fluorescence of binding-site fragments of the nicotinic acetylcholine receptor Perturbations produced upon binding a-bungarotoxin, Biochemistry 29, 10649-10659 (1990). [Pg.63]

Structure of fluorescent probes that have been used to study ligand binding to the Torpedo nicotinic acetylcholine receptor... [Pg.146]

Herz, J.M. Atherton, S.J. Steric factors limit access to the non-competitive inhibitor site of the nicotinic acetylcholine receptor. Fluorescence Studies. Biophys. J. 1992, 62, 74—76. [Pg.3126]

Johnson, D.A. C-terminus of a long alpha-neurotoxin is highly mobile when bound to the nicotinic acetylcholine receptor a time-resolved fluorescence anisotropy approach. Biophys. Chem 116, 213-218 (2005)... [Pg.291]

Kim, J. McNamee, M. G. Topological disposition of Cys 222 in the a-subunit of nicotinic acetylcholine receptor analyzed by fluorescence-quenching and electron paramagnetic resonance measurements. Biochemistry 1998, 37, 4680-4686. [Pg.357]


See other pages where Fluorescence nicotinic acetylcholine receptor is mentioned: [Pg.49]    [Pg.134]    [Pg.134]    [Pg.202]    [Pg.3114]    [Pg.3116]    [Pg.455]    [Pg.1040]    [Pg.357]    [Pg.115]    [Pg.255]    [Pg.158]    [Pg.201]   
See also in sourсe #XX -- [ Pg.145 , Pg.146 ]




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