publication . Article . 2015

Specific interactions between alkali metal cations and the KcsA channel studied using ATR-FTIR spectroscopy.

Yuji Furutani; Hirofumi Shimizu; Yusuke Asai; Shigetoshi Oiki; Hideki Kandori;
Open Access English
  • Published: 01 Sep 2015 Journal: Biophysics and Physicobiology, volume 12, pages 37-45 (eissn: 2189-4779, Copyright policy)
  • Publisher: The Biophysical Society of Japan (BSJ)
The X-ray structure of KcsA, a eubacterial potassium channel, displays a selectivity filter composed of four parallel peptide strands. The backbone carbonyl oxygen atoms of these strands solvate multiple K(+) ions. KcsA structures show different distributions of ions within the selectivity filter in solutions containing different cations. To assess the interactions of cations with the selectivity filter, we used attenuated total reflection Fourier-transform infrared (ATR-FTIR) spectroscopy. Ion-exchange-induced ATR-FTIR difference spectra were obtained by subtracting the spectrum of KcsA soaked in K(+) solution from that obtained in Li(+), Na(+), Rb(+), and Cs(+...
free text keywords: Regular Article, Vibrational spectroscopy, Ion-protein interaction, Ion selectivity, Coordination chemistry, Biophysics, Crystal structure, Infrared spectroscopy, Ion, Chemistry, Alkali metal, KcsA potassium channel, Coordination complex, chemistry.chemical_classification, Amide, chemistry.chemical_compound, Crystallography, Spectroscopy, Analytical chemistry
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publication . Article . 2015

Specific interactions between alkali metal cations and the KcsA channel studied using ATR-FTIR spectroscopy.

Yuji Furutani; Hirofumi Shimizu; Yusuke Asai; Shigetoshi Oiki; Hideki Kandori;