. Author manuscript; available in PMC: 2011 Jul 27.

Published in final edited form as: Biochemistry. 2010 Jul 27;49(29):5978–5988. doi: 10.1021/bi1004359

Table 2.

Observed thermodynamic parameters for the binding of ERE duplex to wildtype and various mutant constructs of the DB domain of ERα in Phosphate buffer at pH 7.0 and 25°C

	K_obs/nM	ΔH_obs/kcal.mol⁻¹	TΔS_obs/kcal.mol⁻¹	ΔG_obs/kcal.mol⁻¹
DB_WT	43 ± 13	−30.52 ± 0.27	−20.44 ± 0.38	−10.08 ± 0.20
DB_D190A	67 ± 6	−62.05 ± 1.64	−52.33 ± 1.48	−9.80 ± 0.06
DB_H196A	190 ± 24	−23.95 ± 0.08	−14.76 ± 0.14	−9.18 ± 0.07
DB_E203A	172 ± 48	−24.97 ± 1.81	−15.66 ± 1.97	−9.26 ± 0.17
DB_AA	387 ± 90	−23.77 ± 2.29	−15.00 ± 2.36	−8.77 ± 0.14
DB_S193A	102 ± 10	−45.10 ± 1.29	−35.54 ± 1.25	−9.55 ± 0.04
DB_Y197A	316 ± 7	−31.12 ± 0.41	−22.24 ± 0.37	−8.88 ± 0.02
DB_S201A	119 ± 9	−28.70 ± 0.69	−19.23 ± 0.64	−9.46 ± 0.05
DB_K206A	313 ± 6	−30.86 ± 0.86	−21.97 ± 0.85	−8.89 ± 0.07
DB_K210A	326 ± 11	−25.96 ± 0.17	−17.09 ± 0.18	−8.86 ± 0.09
DB_R211A	745 ± 76	−8.21 ± 0.09	+0.17 ± 0.10	−8.38 ± 0.11

The various constructs of the DB domain are the wildtype consruct (DB_WT), the single mutant constructs (DB_D190A, DB_H196A, DB_E203A, DB_S193A, DB_Y197A, DB_S201A, DB_K206A, DB_K210A, DB_R211A) and the H196A/E203A double mutant construct (DB_AA). The binding stoichiometries to the fits agreed to within ±10%. Errors were calculated from 3–4 independent measurements. All errors are given to one standard deviation.