TABLE 3.
Thermodynamics properties for Cu(II) binding to wtPAI‐1 and variants at 10°C
| PAI‐1 variant | Model (n) | K obs, M−1 | K d a | ΔG obs, (kcal/Mol) b | ΔH obs , (kcal/mol) | −TΔS obs, (kcal/Mol) c |
|---|---|---|---|---|---|---|
| Active wt | 1 | 1.9 (±0.9) × 107 | 59.5 (±27.6) nM | −9.4 (±0.3) | −17.1 (±0.1) | 7.7 (±0.3) |
| Latent wt | 2 |
1.9 (±0.2) × 107 1.7 (±1.0) × 104 |
52.0 (±7.1) nM 73.6 (±45.6) μM |
−9.4 (±0.1) −5.4 (±0.4) |
−12.1 (±0.1) −12.9 (±1.0) |
2.6 (±0.1) 7.5 (±0.6) |
| Active H10A | 1 | 1.2 (±0.3) × 107 | 87.8 (±23.3) nM | −9.2 (±0.2) | −18.4 (±0.1) | 9.3 (±0.2) |
| Latent H10A | 2 |
1.5 (±0.6) × 107 2.3 (±1.3) × 104 |
74.6 (±32.3) nM 36.0 (±7.5) μM |
−9.3 (±0.3) −5.6 (±0.4) |
−11.9 (±0.1) −24.2 (±4.6) |
2.6 (±0.2) 18.6 (±4.2) |
| Active E81A | 2 |
5.7 (±0.9) × 107 2.5 (±1.8) × 104 |
17.0 (±2.8) nM 53.7 (±39.1) μM |
−10.1 (±0.1) −5.6 (±0.5) |
−17.5 (±0.1) −15.7 (±5.6) |
7.4 (±0.1) 10.1 (±5.2) |
| Latent E81A | 2 |
2.8 (±0.1) × 107 1.2 (±0.1) × 104 |
36.0 (±0.1) nM 83.0 (±7.8) μM |
−9.6 (±0.1) −5.3 (±0.1) |
−14.7 (±1.0) −15.3 (±2.0) |
5.0 (±1.0) 10.1 (±2.1) |
| Active H364A | 1 | 3.5 (±1.2) × 105 | 3.0 (±1.0) μM | −7.3 (±0.2) | −33.1 (±3.8) d | 25.4 (±4.4) d |
| Latent H364A | 1 | 4.8 (±0.7) × 104 | 21.2 (±3.3) μM | −6.1 (±0.1) | −43.9 (±8.6) d | 37.8 (±8.7) d |
| Active H2AH3A e | 1 | 4.2 (±0.9) × 104 | 24.0 (±5.0) μM | −6.0 (±0.1) | −20.0 (±12.0) d | 14.0 (±12.0) d |
| Latent H2AH3A e | 1 | 7.7 (±4.6) × 104 | 13.0 (±6.0) μM | −6.3 (±0.4) | −16.4 (±0.6) d | 10.0 (±0.4) d |
K d calculated from the following relationship: Kd = 1/Kobs.
ΔG ob s calculated from ΔGobs = −RT ln Kobs.
−TΔS obs term calculated from ΔGobs = ΔHobs − TΔSobs.
Parameters measured at the low sensitivity limit of the ITC and likely have significant error associated with them.
Values previously published (Bucci JC, McClintock CS, Chu Y, Ware GL, McConnell KD, Emerson JP, Peterson CB (2017) J Biol Inorg Chem 22 (7):1123–1,135).