TABLE 1.
ETV6-SAM domain dimerization quantitated by ITC
ITC experiments were conducted with SAM domains in 20 mm MOPS, 50 mm NaCl, 0.5 mm EDTA at pH 8.0 and at 25 °C. The tabulated values for the stoichiometry (N), equilibrium dissociation constant (Kd), and enthalpy (ΔHo) and entropy (ΔSo) changes for dimerization are the mean and S.D. of three independent titrations.
| Protein in syringe | Protein in cell | N | Kd | ΔHo | ΔSo |
|---|---|---|---|---|---|
| nm | kcal/mol | cal/mol deg | |||
| A93D | V112E | 0.90 ± 0.03 | 4.4 ± 2.2 | −8.4 ± 0.2 | 10 ± 1.0 |
| A93D | V112E/K99R | 0.94 ± 0.05 | 6.4 ± 1.6 | −7.3 ± 0.3 | 13 ± 0.8 |
| A93D/K99R | V112E | 0.98 ± 0.19 | 1900 ± 1200 | −2.0 ± 1.0 | 19 ± 5 |