Publication Type Academic Article
Authors Hinton J, Fernandez J, Shungu D, Millett F
Journal Biophys J
Volume 55
Issue 2
Pagination 327-30
Date Published 02/01/1989
ISSN 0006-3495
Keywords Gramicidin, Lipid Bilayers, Lysophosphatidylcholines, Models, Biological
Abstract Thermodynamic parameters, enthalpy and entropy, for the binding of the divalent cations, Mg+2, Ca+2, Sr+2, Ba+2, and Cd+2, to gramicidin A, incorporated into lysophosphatidylcholine, have been determined using a combination of Tl-205 nuclear magnetic resonance spectroscopy and competition binding. The binding process is thermodynamically driven by the enthalpy and not the entropy. The enthalpy values are related to the process involving the transfer of cations from an aqueous environment to an amide environment. A comparison is made between the thermodynamic parameters for the binding of monovalent and divalent cations to gramicidin A to illustrate the channel blocking ability of the divalent cations with respect to monovalent cation transport.
DOI 10.1016/S0006-3495(89)82808-5
PubMed ID 2469486
PubMed Central ID PMC1330474
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