. Author manuscript; available in PMC: 2016 Aug 1.

Published in final edited form as: Biochemistry. 2016 Mar 15;55(12):1741–1748. doi: 10.1021/acs.biochem.5b01122

Table 1. Thermodynamic parameters obtained from ITC measurements for the binding of RXRα homodimer to DR1 response elements.

Dimer	Kd (nM)	N	ΔH_obs kcal.mol⁻¹	ΔS_obs cal x mol^-1 x deg^-1
RXRα DBD	38 ± 15	1.1	-39 ± 3	-98
Ramp2 DR1	38 ± 15	1.1	-39 ± 3	-98
RXRα NTD-DBD	93 ± 15	1.01	-28 ± 0.7	-63
Ramp2 DR1	93 ± 15	1.01	-28 ± 0.7	-63
RXRα ΔNTD	47 ± 4	1.08	-28 ± 1	-58
Ramp2 DR1	47 ± 4	1.08	-28 ± 1	-58
RXRα full-length	79 ± 15	1.0	-24 ± 2	-49
Ramp2 DR1	79 ± 15	1.0	-24 ± 2	-49

Errors were calculated from 3 independent measurements performed at 298 K. All uncertainties are given to one standard deviation. N corresponds to the number of moles of dimer per mole of DNA. Concentrations were measured by UV spectrophometry.