. 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 1.

Observed thermodynamic parameters for the binding of ERE duplex to the wildtype DB domain of ERα in various buffers 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
Phosphate	43 ± 13	−30.52 ± 0.27	−20.44 ± 0.38	−10.08 ± 0.20
Hepes	59 ± 6	−17.22 ± 0.50	−7.34 ± 0.53	−9.88 ± 0.07
Tricine	238 ± 84	−6.06 ± 1.54	+3.02 ± 1.68	−9.08 ± 0.23
Tris	336 ± 6	+9.82 ± 0.64	+19.10 ± 0.52	−8.94 ± 0.12

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.