. Author manuscript; available in PMC: 2013 Mar 13.

Published in final edited form as: Biochemistry. 2012 Mar 2;51(10):2122–2135. doi: 10.1021/bi3000534

Table 2.

Thermodynamic parameters obtained from ITC measurements for the binding of wildtype (WT) and mutant constructs of the PR domain of Sos1 to full-length Grb2

	n	K_d (µM)	ΔH (kcal.mol⁻¹)	TΔS (kcal.mol⁻¹)	ΔG (kcal.mol⁻¹)
PR_WT	2.12 ± 0.03	7.02 ± 0.04	−39.85 ± 0.28	−25.77 ± 0.29	−14.08 ± 0.01
PR_mS1	1.94 ± 0.01	8.99 ± 0.51	−39.81 ± 0.59	−26.03 ± 0.66	−13.78 ± 0.07
PR_mS2	2.02 ± 0.05	6.98 ± 0.30	−34.11 ± 0.25	−20.03 ± 0.20	−14.08 ± 0.05
PR_mS3	2.04 ± 0.02	2.40 ± 0.03	−38.39 ± 0.33	−23.04 ± 0.32	−15.35 ± 0.01
PR_mS4	2.01 ± 0.02	6.18 ± 0.27	−38.17 ± 0.10	−23.94 ± 0.05	−14.23 ± 0.05
PR_mS12	2.05 ± 0.04	19.57 ± 0.27	−37.06 ± 0.11	−24.20 ± 0.09	−12.86 ± 0.02
PR_mS13	2.14 ± 0.02	10.14 ± 0.05	−36.55 ± 0.08	−22.91 ± 0.08	−13.64 ± 0.01
PR_mS14	1.14 ± 0.01	15.48 ± 0.10	−17.55 ± 0.22	−11.06 ± 0.21	−6.57 ± 0.01
PR_mS23	2.00 ± 0.01	12.67 ± 0.15	−34.56 ± 0.04	−21.18 ± 0.05	−13.37 ± 0.01
PR_mS24	1.89 ± 0.02	11.76 ± 0.70	−32.52 ± 0.64	−19.05 ± 0.71	−13.46 ± 0.07
PR_mS34	1.00 ± 0.01	2.29 ± 0.12	−17.53 ± 0.42	−9.82 ± 0.44	−7.70 ± 0.03
PR_mS123	1.07 ± 0.05	37.28 ± 3.62	−20.09 ± 0.03	−14.04 ± 0.03	−6.05 ± 0.06
PR_mS124	1.03 ± 0.04	101.44 ± 2.04	−14.61 ± 0.13	−9.15 ± 0.12	−5.45 ± 0.01
PR_mS134	1.05 ± 0.01	29.98 ± 1.65	−18.14 ± 0.25	−11.96 ± 0.28	−6.18 ± 0.03
PR_mS234	1.03 ± 0.02	44.96 ± 1.29	−16.88 ± 0.12	−10.94 ± 0.10	−5.94 ± 0.02

Note that n is the stoichiometry of full-length Grb2 bound to each PR construct. Errors were calculated from at least three independent measurements. All errors are given to one standard deviation.