Thallium-205 NMR determination of the thermodynamics of the interaction between the thallous ion and gramicidin dimers incorporated into micelles.
A study has been made of the thermodynamics of the interaction between the thallous ion and gramicidin dimers incorporated into micelles using thallium-205 NMR spectroscopy. The chemical shift data obtained are interpreted interms of a model in which the dimer has only one tight binding site. The variation of the binding constant over the temperature range 303-323 K is used to determine the changes in enthalpy and entropy of binding giving values of -11.3 kcal/mole and -16 e.u. at 303 K, respectively.
D003102:Colloids; D006096:Gramicidin; D007473:Ion Channels / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008954:Models, Biological; D011487:Protein Conformation; D013793:Thallium; D013816:Thermodynamics
D003102:Colloids; D007473:Ion Channels; D008823:Micelles; D006096:Gramicidin; D013793:Thallium