Thermodynamics of Cation Binding and Transport by Gramidicin
Conference paper
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.
Keywords
Monovalent Cation Channel Entrance Cation Binding Cation Radius Equilibrium Binding Constant
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