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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : FEBS letters

Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 25 Sep 2002

Martinez KL, Gohon Y, Corringer PJ, Tribet C, Mérola F, Changeux JP, Popot JL

Link to Pubmed [PMID] – 12297315

FEBS Lett. 2002 Sep;528(1-3):251-6

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.

http://www.ncbi.nlm.nih.gov/pubmed/12297315