Figure 4.
Figure 4. K+ binding competition examined by ITC. Potassium to protein titration in the presence of different cations. (a) KCl titration to protein solution in 195 mM choline-Cl with 5 mM NaCl reveals an apparent Kd of 0.26 mM. (b–d) KCl titration to protein solutions that contain 50 mM NaCl, RbCl, or CsCl in 150 mM LiCl solution buffered with 20 mM Tris-HCl, pH 7.5. The lower panels giving the integrated injection heat pulses, normalized per mole of injection, reveal different binding curves fitted by one-site binding model. Individual Kd values derived from fitting ± SE are indicated. Each graph represents an example of three independent experiments.

K+ binding competition examined by ITC. Potassium to protein titration in the presence of different cations. (a) KCl titration to protein solution in 195 mM choline-Cl with 5 mM NaCl reveals an apparent Kd of 0.26 mM. (b–d) KCl titration to protein solutions that contain 50 mM NaCl, RbCl, or CsCl in 150 mM LiCl solution buffered with 20 mM Tris-HCl, pH 7.5. The lower panels giving the integrated injection heat pulses, normalized per mole of injection, reveal different binding curves fitted by one-site binding model. Individual Kd values derived from fitting ± SE are indicated. Each graph represents an example of three independent experiments.

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