Table 1.
Homo-dimerization affinities from AUC measurements at 25°C
| Protein | Description | KA (x 104) M−1 | Ref. |
|---|---|---|---|
| Xenopus C-cadherin EC1–5 | |||
| WT | Wild Type | 1.56 | [48] |
| Mouse E-cadherin EC1–2 | |||
| WT | Wild Type (human) | 1.25 | [49] |
| WT | Wild Type | 1.04 | [4] |
| WT | Wild Type | 1.01 | [16] |
| W2A | Strand-swap mutant | 0.11 | |
| Ala-Ala N-terminal extension | Strand-swap mutant | 0.12 | |
| E89A | Strand-swap mutant | 0.34 | |
| Asp-Trp deletion at N-terminus | Strand-swap mutant | 0.15 | |
| K14E | X-dimer mutant | 1.17 | |
| K14S | X-dimer mutant | 1.04 | |
| Y142R | X-dimer mutant | 1.30 | |
| W2A K14E | Double mutant | monomer | |
| W2F | Reduced strain on A*/A strand | 0.41 | [17] |
| Ala inserted between 2 and 3 | Reduced strain on A*/A strand | 0.07 | |
| AlaAla inserted between 2 and 3 | Reduced strain on A*/A strand | 0.51 | |
| E11D | Enhanced strand-swapping | 1.40 | |
| P5A P6A | Swapping strand stabilization | 27 | |
| P5S P6S | Swapping strand stabilization | 34 | |
| P5G P6G | Swapping strand stabilization | 37 | |
| P5A | Swapping strand stabilization | 34 | |
| P5G | Swapping strand stabilization | 21 | |
| Mouse N-cadherin EC1–2 | |||
| WT | Wild Type | 3.88 | [4] |
| P5A P6A | Swapping strand stabilization | 27 | [17] |