Publication Type Academic Article
Authors Hinton J, Fernandez J, Shungu D, Whaley W, Koeppe R, Millett F
Journal Biophys J
Volume 54
Issue 3
Pagination 527-33
Date Published 09/01/1988
ISSN 0006-3495
Keywords Gramicidin, Ion Channels, Models, Biological
Abstract Thermodynamic parameters for the binding of the monovalent cations, Li+, Na+, K+, Rb+, Cs+, NH4+, TI+, and Ag+, to gramicidin A and for the binding of TI+ to gramicidin C, incorporated into lysophosphatidylcholine, have been determined using a combination of TI-205 nuclear magnetic resonance spectroscopy and competition binding. The thermodynamic parameters, enthalpy and entropy, are discussed in terms of a process involving the transfer of cations from an aqueous to amide environment.
DOI 10.1016/S0006-3495(88)82985-0
PubMed ID 2462930
PubMed Central ID PMC1330351
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