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

Biophys J. 1988 Sep;54(3):527-33. doi: 10.1016/S0006-3495(88)82985-0.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Gramicidin / metabolism*
  • Ion Channels / physiology*
  • Magnetic Resonance Spectroscopy / methods
  • Models, Biological*
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Thallium
  • Thermodynamics

Substances

  • Ion Channels
  • Gramicidin
  • Thallium