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

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Standard

Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols : Molecular interactions vs. physical constraints. / Martinez, Karen L.; Gohon, Yann; Corringer, Pierre Jean; Tribet, Christophe; Mérola, Fabienne; Changeux, Jean Pierre; Popot, Jean Luc.

I: FEBS Letters, Bind 528, Nr. 1-3, 25.09.2002, s. 251-256.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Martinez, KL, Gohon, Y, Corringer, PJ, Tribet, C, Mérola, F, Changeux, JP & Popot, JL 2002, 'Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints', FEBS Letters, bind 528, nr. 1-3, s. 251-256. https://doi.org/10.1016/S0014-5793(02)03306-9

APA

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

Vancouver

Martinez KL, Gohon Y, Corringer PJ, Tribet C, Mérola F, Changeux JP o.a. Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints. FEBS Letters. 2002 sep. 25;528(1-3):251-256. https://doi.org/10.1016/S0014-5793(02)03306-9

Author

Martinez, Karen L. ; Gohon, Yann ; Corringer, Pierre Jean ; Tribet, Christophe ; Mérola, Fabienne ; Changeux, Jean Pierre ; Popot, Jean Luc. / Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols : Molecular interactions vs. physical constraints. I: FEBS Letters. 2002 ; Bind 528, Nr. 1-3. s. 251-256.

Bibtex

@article{982a523f2fbe4b59a9111be7f516008f,
title = "Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints",
abstract = "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.",
keywords = "Amphipol, Conformational transition, Detergent, Membrane protein, Nicotinic acetylcholine receptor",
author = "Martinez, {Karen L.} and Yann Gohon and Corringer, {Pierre Jean} and Christophe Tribet and Fabienne M{\'e}rola and Changeux, {Jean Pierre} and Popot, {Jean Luc}",
year = "2002",
month = sep,
day = "25",
doi = "10.1016/S0014-5793(02)03306-9",
language = "English",
volume = "528",
pages = "251--256",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-3",

}

RIS

TY - JOUR

T1 - Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols

T2 - Molecular interactions vs. physical constraints

AU - Martinez, Karen L.

AU - Gohon, Yann

AU - Corringer, Pierre Jean

AU - Tribet, Christophe

AU - Mérola, Fabienne

AU - Changeux, Jean Pierre

AU - Popot, Jean Luc

PY - 2002/9/25

Y1 - 2002/9/25

N2 - 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.

AB - 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.

KW - Amphipol

KW - Conformational transition

KW - Detergent

KW - Membrane protein

KW - Nicotinic acetylcholine receptor

U2 - 10.1016/S0014-5793(02)03306-9

DO - 10.1016/S0014-5793(02)03306-9

M3 - Journal article

C2 - 12297315

AN - SCOPUS:0037174145

VL - 528

SP - 251

EP - 256

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-3

ER -

ID: 131611430