title: TI-205 nuclear magnetic resonance determination of the thermodynamic parameters for the binding of monovalent cations to gramicidins A and C.
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.
authors: Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville 72701.
authors: J F
authors: JF
authors: Hinton
authors: J Q
authors: JQ
authors: Fernandez
authors: D C
authors: DC
authors: Shungu
authors: W L
authors: WL
authors: Whaley
authors: R E
authors: RE
authors: Koeppe
authors: F S
authors: FS
authors: Millett
mesh_terms: D006096:Gramicidin / Q000378:metabolism*; D007473:Ion Channels / Q000502:physiology*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008954:Models, Biological; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D013793:Thallium; D013816:Thermodynamics
chemical_list: D007473:Ion Channels; D006096:Gramicidin; D013793:Thallium