Skip to main content
. 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 3.

Thermodynamic parameters for the binding of ZRE duplex to the double-mutant DB domain containing the E354H/E410H substitutions (DB_HH) of EGR1 at various pH

Kd/nM ΔH/kcal.mol−1 TΔS/kcal.mol−1 ΔG/kcal.mol−1
pH 5.0 5456 ± 1079 −21.39 ± 0.61 −14.20 ± 0.50 −7.19 ± 0.12
pH 5.5 3860 ± 645 −20.39 ± 0.40 −12.99 ± 0.29 −7.40 ± 0.10
pH 6.0 3736 ± 1076 −14.87 ± 0.57 −7.45 ± 0.74 −7.42 ± 0.17
pH 6.5 2177 ± 696 −9.37 ± 0.33 −1.63 ± 0.14 −7.75 ± 0.19
pH 7.0 192 ± 18 −5.57 ± 0.20 +3.75 ± 0.14 −9.17 ± 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.