Investigation of the interaction between thallous ions and gramicidin A in dimyristoylphosphatidylcholine vesicles: a thallium-205 NMR equilibrium study. Academic Article uri icon

Overview

abstract

  • This study reports the first direct observation of multiple occupancy of the gramicidin A channel by Tl+ ions. 205Tl NMR has been used to study the equilibrium binding of Tl+ by gramicidin A incorporated in sonicated dimyristoylphosphatidylcholine vesicles. It is shown that only multiple-channel occupancy can account for the 205Tl chemical shifts measured. The data are analyzed to yield the equilibrium association constants of 450-600 and 5-20 M-1 for the binding of the first and the second ions at 34 degrees C, respectively.

publication date

  • October 7, 1986

Research

keywords

  • Dimyristoylphosphatidylcholine
  • Gramicidin
  • Liposomes
  • Thallium

Identity

Scopus Document Identifier

  • 0022996029

Digital Object Identifier (DOI)

  • 10.1021/bi00368a040

PubMed ID

  • 2431708

Additional Document Info

volume

  • 25

issue

  • 20