The binding of a fluorescent agonist to the acetycholine receptor from Torpedo electric organ has been studied by time-resolved spectroscopy in three different environments: in native membrane fragments, in the detergent CHAPS, and after complexation by amphipathic polymers ('amphipols'). Binding kinetics was similar in the membrane and in amphipols, demonstrating that the receptor can display unaltered allosteric transitions outside its natural lipid environment. In contrast, allosteric equilibria were strongly shifted towards the desensitized state in CHAPS. Therefore, the effect of CHAPS likely results from molecular interactions rather than from the loss of bulk physical properties of the membrane environment. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Martinez, K. L., Gohon, Y., Corringer, P. J., Tribet, C., Mérola, F., Changeux, J. P., & Popot, J. L. (2002). Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints. FEBS Letters, 528(1–3), 251–256. https://doi.org/10.1016/S0014-5793(02)03306-9