TI-205 nuclear magnetic resonance determination of the thermodynamic parameters for the binding of monovalent cations to gramicidins A and C.

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