TABLE 1.
Thermodynamic data from ITC analysis of the VPg-3D binding reaction
| VPga | Kd (μM)b | ΔΗ (Kcal/mol) | TΔS (Kcal/mol) | N |
|---|---|---|---|---|
| WT | 11.3 ± 0.9 | −10.2 ± 0.2 | −4.0 ± 0.3 | 1.21 ± 0.06 |
| Y3A | 4.7 ± 0.3 | −12.60 ± 0.06 | −5.84 ± 0.01 | 0.84 ± 0.01 |
| T4A | 6.5 ± 0.2 | −10.77 ± 0.01 | −4.19 ± 0.02 | 1.09 ± 0.01 |
| K9A | 16 ± 2 | −10.7 ± 0.4 | −4.6 ± 0.5 | 1.19 ± 0.02 |
| V13A | 7.2 ± 1.1 | −9.6 ± 0.5 | −3.1 ± 0.6 | 1.28 ± 0.02 |
| P14A | NB | |||
| T15A | 22 ± 5 | −9.2 ± 0.7 | −3.3 ± 0.8 | 1.09 ± 0.06 |
| I16A | 30 ± 2 | −9.5 ± 0.3 | −3.8 ± 0.4 | 1.07 ± 0.08 |
| R17A | NB | |||
| R17K | NB | |||
| K20A | 17.0 ± 1.2 | −10.16 ± 0.18 | −4.1 ± 0.2 | 1.58 ± 0.13 |
a
Isothermal titration analysis of the L446D R455D mutant of poliovirus 3D with either wild-type VPg (WT) or VPg containing the indicated mutation.
b
ΔH, change in enthalpy; ΔS, change in entropy; N, stoichiometry of the binding reaction; NB, no appreciable binding was detected; T, 277 K.