Table 2.

Temperature-Dependence of Thermodynamic Parameters for the Binding of Actinonin to PDF_Ec^a,^b

Temperature (°C)	n	ΔH° (kcal mol−1)	ΔG° (kcal mol−1)	TΔS° (kcal mol−1)
10	0.26 ± 0.003	−0.3 ± 0.1	−10.5	10.2
	0.76 ± 0.009	6.3 ± 0.1	−7.7	14.1
15	0.29 ± 0.002	−1.1 ± 0.08	−11.5	10.3
	0.76 ± 0.007	5.5 ± 0.07	−8.1	13.6
20	0.29 ± 0.002	−2.1 ± 0.07	−12.0	9.9
	0.78 ± 0.008	4.4 ± 0.07	−8.4	12.8
25	0.29 ± 0.002	−3.3 ± 0.06	−12.2	8.9
	0.73 ± 0.007	3.8 ± 0.06	−8.6	12.4
30	0.32 ± 0.001	−3.9 ± 0.03	−12.5	8.6
	0.76 ± 0.005	2.8 ± 0.04	−9.0	11.6
35	0.29 ± 0.002	−5.1 ± 0.08	−12.4	7.2
	0.76 ± 0.02	1.7 ± 0.06	−9.2	10.8

^ain 50 mM potassium phosphate buffer, 1mM NiCl₂, pH 7.0. n refers to the stoichiometry of actinonin-PDF_Ec complex (mol/mol).

^bFor each temperature the upper row lists thermodynamic parameters for the higher-affinity site whereas the bottom row lists those for the lower-affinity site.