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Walcher, S. ; Altschuh, J. ; Sandermann, H.

The Lipid/Protein Interface as Xenobiotic Target Site : Kinetic Analysis of the Nicotinic Acetylcholine Receptor.

J. Biol. Chem. 276, 42191-42195 (2001)
Verlagsversion DOI
Open Access Gold
Membrane proteins are known to be solvated and functionally activated by a fixed number of lipid molecules whose multiple binding can be described by Adair-type binding equations. Lipophilic xenobiotics such as general anesthetics may act by competitive displacement of protein-bound lipids. A kinetic equation is now presented for various binding stoichiometries of lipid and xenobiotic, and microscopic binding constants of anesthetics and organic solvents are derived from two independent assay systems for the enhancement of agonist binding to the nicotinic acetylcholine receptor. These constants lead to the first available free energy estimate (−6.4 kcal/mol) for the binding of membrane lipid to an integral membrane protein.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache englisch
Veröffentlichungsjahr 2001
HGF-Berichtsjahr 0
ISSN (print) / ISBN 0021-9258
e-ISSN 1083-351X
Zeitschrift Journal of Biological Chemistry, The
Quellenangaben Band: 276, Heft: , Seiten: 42191-42195 Artikelnummer: , Supplement: ,
Verlag American Society for Biochemistry and Molecular Biology
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Biomathematics and Biometry (IBB)
Institute of Biochemical Plant Pathology (BIOP)
DOI 10.1074/jbc.M105136200
Erfassungsdatum 2001-12-31
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