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. Author manuscript; available in PMC: 2014 Aug 1.
Published in final edited form as: FEBS J. 2013 Jun 18;280(15):3669–3684. doi: 10.1111/febs.12360

Table 1.

Thermodynamic parameters for the binding of ZRE duplex to wildtype DB domain (DB_WT) of EGR1 at various pH

Kd/nM ΔH/kcal.mol−1 TΔS/kcal.mol−1 ΔG/kcal.mol−1
pH 5.0 1962 ± 485 −33.43 ± 0.73 −25.63 ± 0.58 −7.80 ± 0.15
pH 5.5 2045 ± 363 −31.01 ± 0.68 −23.23 ± 0.57 −7.77 ± 0.11
pH 6.0 806 ± 77 −25.26 ± 0.30 −16.94 ± 0.25 −8.32 ± 0.06
pH 6.5 311 ± 30 −22.49 ± 0.65 −13.60 ± 0.70 −8.89 ± 0.06
pH 7.0 236 ± 27 −18.71 ± 0.46 −9.67 ± 0.39 −9.05 ± 0.07
pH 7.5 186 ± 16 −14.34 ± 0.31 −5.15 ± 0.25 −9.19 ± 0.05
pH 8.0 149 ± 15 −4.53 ± 0.34 +4.80 ± 0.28 −9.32 ± 0.06

The binding stoichiometries to the fits agreed to within ±10%. Errors were calculated from at least three independent measurements. All errors are given to one standard deviation.