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. 2009 May 20;96(10):4144–4152. doi: 10.1016/j.bpj.2009.02.015

Figure 4.

Figure 4

The binding of HMGA2 to FL-AT-1 is an entropy-driven reaction. (A) Sample raw data for the titration of HMGA2 into FL-AT-1 at 5°C in 1 × BPE containing 200 mM of NaCl (total 216 mM Na+). Top: each peak shows the heat produced by injection of an aliquot of 15 μL of HMGA2 (35.7 μM) into DNA solution (1.44 mL of 5 μM). Bottom: the binding isotherm generated from integration with respect of time with appropriate dilution correction. (B) Heat capacity change (ΔCp) for binding HMGA2 to FL-AT-1. Linear least-squares fitting of the enthalpy data (up triangles) determined by ITC giving a ΔCp value of −330 (±30) cal mol−1 K−1. The dependence of ΔG (circles) and −TΔS (down triangles) on temperature are shown. The standard deviation of ΔH at different temperatures was estimated to be 0.1 (5°C), 0.1 (10°C), 0.2 (15°C), 0.3 (20°C), and 0.2 (25°C) kcal mol−1, respectively.