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. 2015 Jul 10;290(34):20856–20864. doi: 10.1074/jbc.M115.659136

FIGURE 4.

FIGURE 4.

ITC and SAXS analysis of nucleotide binding to BipA. A and B, isothermal titration calorimetry curves of BipA titrated with GDP (A) and ppGpp (B) after correction of the dilution effect of nucleotides. C, enthalpy change for the GDP (open circles) and ppGpp binding (filled circles) to BipA as a function of temperature (°C). D, entropy change for the GDP (open circles) and ppGpp binding (filled circles) to BipA as a function of the logarithm of temperature in Kelvin. The heat capacity change (ΔCp) value from the enthalpy (C) is similar to that obtained from entropy (D). E, the unique scattering profiles of the apo BipA, in yellow, BipA with bound GDP, in green, and BipA with bound ppGpp, in blue, are shown with intensity (I), plotted against the photon momentum transfer (q). F, the P(r) distribution functions of apo BipA, in yellow, BipA with bound GDP, in green, and BipA with bound ppGpp, in blue, are depicted.