Table 1.
Mutational data for the FBP WW domain
| Mutation | Φexp | ΔGN,exp | Affected elements |
|---|---|---|---|
| E7A | 0.67 ± 0.21 | 0.52 ± 0.16 | hp 1 |
| W8F | 0.24 ± 0.03 | 1.65 ± 0.16 | hp 1, hc |
| T9A | −0.09 ± 0.04 | 0.93 ± 0.09 | hp 1 |
| T9G | 0.94 ± 0.20 | 0.50 ± 0.10 | hp 1 |
| Y11A | 0.55 ± 0.10 | 0.63 ± 0.11 | hp 1 |
| T13A | −0.03 ± 0.07 | 0.81 ± 0.17 | hp 1, hc |
| T13G | −0.32 ± 0.25 | 0.58 ± 0.22 | hp 1, hc |
| A14G | 0.69 ± 0.28 | 0.50 ± 0.22 | hp 1 |
| D15A | 0.82 ± 0.16 | 0.42 ± 0.09 | hp 1 |
| D15G | 0.77 ± 0.17 | 0.39 ± 0.09 | hp 1 |
| G16A | 1.17 ± 0.22 | 1.33 ± 0.27 | hp 1 |
| T18A | 0.93 ± 0.27 | 0.54 ± 0.17 | hp 1 |
| T18G | 0.73 ± 0.05 | 1.14 ± 0.09 | hp 1 |
| Y19A | 0.11 ± 0.05 | 0.67 ± 0.13 | hp 1, hp 2 |
| Y20F | 0.05 ± 0.16 | 0.68 ± 0.18 | hp 1, hp 2, hc |
| Y21A | 0.28 ± 0.02 | 1.70 ± 0.10 | hp 1, hp 2 |
| R24A | 0.29 ± 0.09 | 0.78 ± 0.17 | hp 1, hp 2 |
| T25A | 0.39 ± 0.04 | 2.51 ± 0.18 | hp 2 |
| T25S | 0.27 ± 0.03 | 1.08 ± 0.09 | hp 2 |
| L26A | 0.08 ± 0.08 | 0.56 ± 0.12 | hp 2 |
| L26G | 0.45 ± 0.04 | −1.29 ± 0.10 | hp 2 |
| E27A | 0.12 ± 0.04 | 1.02 ± 0.13 | hp 2, hc |
| T29G | 0.09 ± 0.02 | 1.89 ± 0.11 | hp 2, hc |
| W30A | 0.19 ± 0.06 | 0.76 ± 0.14 | hp 2, hc |
| L36A | −0.30 ± 0.16 | 0.91 ± 0.14 | hp 2, hc |
| L36V | −0.13 ± 0.09 | 0.53 ± 0.14 | hp 2, hc |
Experimental Φ-values and stability changes ΔGN,exp are from Petrovich et al. (33). The information on the structural elements affected by the mutations is derived from the contact map shown in Fig. 3. These structural elements are the hairpin 1 (hp 1), hairpin 2 (hp 2), and the small hydrophobic core (hc) of the protein (see text).