Table 1. Association rates (ka), dissociation rates (kd) and dissociation constants (KD) for the interactions of wild-type rBTI and its mutants with bovine trypsin.
| Inhibitor | P8′ residue | P2 residue | Speculated interaction | Reference Model | ka, M−1s−1 | kd, s−1 | KD(kd/ka), M |
| WT rBTI | Trp53 | Pro44 | Hydrophobic force | rBTI | 4.62×105 | 1.25×10−3 | 2.69×10−9 |
| P44T | Trp53 | Thr44 | Hydrogen bond | LUTI | 3.46×105 | 5.24×10−7 | 1.52×10−12 |
| W53R/P44T | Arg53 | Thr44 | Hydrogen bond | CI-2 | 6.79×105 | 5.54×10−4 | 8.15×10−10 |
| W53F | Phe53 | Pro44 | Hydrophobic force | - | 3.99×105 | 2.46×10−3 | 6.16×10−9 |
| W53R | Arg53 | Pro44 | - | - | 6.59×105 | 9.97×10−3 | 1.51×10−8 |