Table 2. Thermodynamics and stability of the target proteins.
The thermodynamic parameters derived from solvent (urea) and thermal denaturation, as well as PK sensitivity are presented for each target. All values are shown as the mean +/− the standard deviation of at least 3 independent experiments. For proteins D6:7 and D16:17, only partial reversibility was demonstrated in the thermal denaturation experiments, so the fitted parameter values are subject to interpretation and should best be viewed as estimates; for this reason those results have been italicized; see text for details.
| Solvent Denaturation | Thermal Denaturation | Proteolysis | ||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| protein | DG kJ./mol | [Urea]mid M | DH kJ/mol | Tm C | Cp J/mol K | PK50 nmol | ||||||||||||
| D4:5 | −32.4 | +/− | 2.2 | 4.36 | +/− | 0.03 | −381 | +/− | 9 | 65.0 | +/− | 0.1 | −12.1 | +/− | 0.5 | 26.5 | +/− | 6.2 |
| D6:7 | −7.9 −25.2 |
+/− +/− |
0.5 2.3 |
1.64 3.84 |
+/− | 0.06 0.07 |
−333 | +/− | 10 | 57.4 | +/− | 0.1 | −11.1 | +/− | 1.2 | 2.8 | +/− | 0.7 |
| D7:8 | ND | ND | ND | ND | ND | 0.15 | +/− | 0.03 | ||||||||||
| D8:9 | ND | ND | −120 | +/− | 6 | 53.8 | +/− | 0.4 | −3.9 | +/− | 0.4 | 0.14 | +/− | 0.04 | ||||
| D16:17 | −46.3 | +/− | 1.1 | 5.07 | +/− | 0.01 | −505 | +/− | 12 | 69.2 | +/− | 0.1 | −15.1 | +/− | 0.6 | 5.5 | +/− | 1.9 |
| D18:19 | −10.7 | +/− | 0.6 | 2.87 | +/− | 0.05 | −289 | +/− | 7 | 59.2 | +/− | 0.1 | 3.5 | +/− | 3.0 | 5.4 | +/− | 2.4 |