Thermodynamic properties of N-terminal mutations used, as determined by ITC
| Protein interaction (cell + syringe) | Kd | ΔH | −TΔS | ΔG | N |
| nM | kcal/mol | kcal/mol | kcal/mol | ||
| ΔN complex + Syb1–96a | 2.1 ± 0.6 | −29.9 ± 0.3 | 18.1 | −11.8 | 1.05 |
| ΔN complex + Syb F77A | 0.8 ± 0.4 | −18.8 ± 0.2 | 6.4 | −12.4 | 0.99 |
| ΔN complex + Syb LATA | 44.1 ± 12.3 | −16.6 ± 0.4 | 6.5 | −10.1 | 1.01 |
| ΔN complex + Syb VAVA | 8.4 ± 2.8 | −23.4 ± 0.4 | 12.3 | −11.1 | 1.02 |
| Protein interaction (cell + syringe) | Kd | ΔH | −TΔS | ΔG | N |
| nM | kcal/mol | kcal/mol | kcal/mol | ||
| ΔN complex + Syb1–96a | 2.1 ± 0.6 | −29.9 ± 0.3 | 18.1 | −11.8 | 1.05 |
| ΔN complex + Syb F77A | 0.8 ± 0.4 | −18.8 ± 0.2 | 6.4 | −12.4 | 0.99 |
| ΔN complex + Syb LATA | 44.1 ± 12.3 | −16.6 ± 0.4 | 6.5 | −10.1 | 1.01 |
| ΔN complex + Syb VAVA | 8.4 ± 2.8 | −23.4 ± 0.4 | 12.3 | −11.1 | 1.02 |
Kd, dissociation constant; ΔH, binding enthalpy; T, absolute temperature in Kelvin; ΔS, entropy change; ΔG, free energy; N, stoichiometry.
These data are from Wiederhold and Fasshauer (2009).