. Author manuscript; available in PMC: 2013 Feb 10.

Published in final edited form as: J Mol Biol. 2011 Dec 14;416(1):57–77. doi: 10.1016/j.jmb.2011.12.015

Table 1.

Thermodynamic parameters for the binding of various BH3 peptides to BclXL_FL and BclXL_dTM constructs

	BclXL_FL				BclXL_dTM
Peptide	K_d/μM	ΔH/kcal.mol⁻¹	TΔS/kcal.mol⁻¹	ΔG/kcal.mol⁻¹	K_d/μM	ΔH/kcal.mol⁻¹	TΔS/kcal.mol⁻¹	ΔG/kcal.mol⁻¹
Bid_BH3	9.97 ± 1.25	−18.74 ± 0.19	−11.91 ± 0.17	−6.82 ± 0.01	0.79 ± 0.08	−6.45 ± 0.07	+1.88 ± 0.03	−8.32 ± 0.04
Bad_BH3	10.30 ± 1.42	−14.19 ± 0.08	−7.37 ± 0.04	−6.81 ± 0.04	0.89 ± 0.12	−7.84 ± 0.14	+0.46 ± 0.11	−8.26 ± 0.02
Bax_BH3	35.10 ± 3.72	−19.40 ± 0.30	−13.31 ± 0.25	−6.08 ± 0.06	3.25 ± 0.27	−5.55 ± 0.07	+1.94 ± 0.08	−7.50 ± 0.01

All parameters were obtained from ITC measurements at pH 8.0 and 25°C. All binding stoichiometries were 1:1 and generally agreed to within ±10%. Errors were calculated from at least three independent measurements. All errors are given to one standard deviation.