Table 2.
Calculated and experimental results for the binding kinetics of PLC-γ SH2 with the Syk linker B peptide in different phosphorylation forms (ionic strength = 155 mM). Each phosphorylation is treated with single protonated phosphate group (net charge of −1).
| Peptides/SH2 | ka0 (105 M−1s−1) | ΔGel* (kcal/mol) | ka (106 M−1s−1) | Fold decrease | Experimental fold decrease8 |
|---|---|---|---|---|---|
| pYpY | 0.39 | −3.84 | 23.8 | ||
| YpY | 0.39 | −2.91 | 5.22 | 4.6 | |
| pYY | 0.39 | −3.26 | 9.40 | 2.5 | 6 |
| YY | 0.39 | −2.30 | 1.89 | 12.6 | |
| βD3 K→Qa | 0.39 | −2.75 | 4.01 | 5.9 | 0.6 |
a
Binding of pYpY to PLC-γ SH2 βD3 K→Q mutant