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. Author manuscript; available in PMC: 2016 Jun 17.
Published in final edited form as: Methods. 2015 Feb 9;76:171–182. doi: 10.1016/j.ymeth.2015.01.012

Fig. 4. Synergistic binding of Cl− ions and H+ to wild type CLC-ec1 (A and B) and to E148A mutant (C and D).

Fig. 4

ITC data for Cl− binding (A and C) in phosphate, HEPES, or Tris buffers. In all experiments buffers were supplemented with 5 mM n-decyl-β,D-maltopyranoside Binding heat rates following baseline subtraction (top) and integrated binding heats (bottom) are shown. The solid lines through the data are fits to a single binding site model. The enthalpy of Cl− binding is plotted as a function of buffer ionization enthalpy (B and C). Error bars are standard errors of the mean. The solid black line in B is a linear fit with slope N = 0.5 ± 0.1. Figures are adapted and modified from Picollo, et al. (12).