Abstract
The thermodynamic parameters for the binding and transport of metal cations have been determined by NMR spectroscopy. A combination of Tl-205 NMR spectroscopy and competitive binding was used to determine the enthalpy and entropy of binding monovalent and divalent cations to the channel entrance of gramicidin A. These thermodynamic parameters are related to the corresponding quantities for the transfer of the Ions from an aqueous to an amide solution. Rates and thermodynamic parameters for the transport of monovalent cations through the channel of gramicidin analogs have been obtained using metal ion NMR spectroscopy.KeywordsMonovalent CationChannel EntranceCation BindingCation RadiusEquilibrium Binding ConstantThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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