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 |