Table 1.
Comparison with published kinetic folding rates
| Construct | λ1, s−1 | A1 (lag) | λ2, s−1 | A2 | λ3, s−1 | A3 | λ4, s−1 | A4 |
|---|---|---|---|---|---|---|---|---|
| H124L† | 38 ± 9 | −0.07 ± 0.01 | 6.2 ± 0.3 | 0.53 ± 0.01 | 0.93 ± 0.07 | 0.22 ± 0.01 | 0.025 ± 0.001 | 0.17 ± 0.003 |
| Pro-† | 99 ± 15 | −0.08 ± 0.01 | 7.8 ± 0.4 | 0.69 ± 0.03 | 2.3 ± 0.2 | 0.24 ± 0.03 | — | — |
| Pro-‡ | 134 ± 21 | −11.3 ± 0.1% | 17.2 ± 0.5 | 57.3 ± 0.9% | 4.7 ± 0.1 | 35.3 ± 1.1% | 0.82 ± 0.04 | 4.5 ± 0.2% |
| WT*§ | 40.6 | −0.23 | 10.4 | 1.78 | 1.35 | 0.4 | 0.1 | 0.26 |
| WT*/Trp76§ | 41.3 | −0.32 | 11.3 | 1.51 | 2.3 | 0.43 | 0.01 | 0.24 |
| P117G/H124L¶ | 47 ± 3 | −0.10 ± 0.01 | 9.7 ± 0.2 | 0.63 ± 0.01 | 2.4 ± 0.1 | 0.17 ± 0.01 | 0.30 ± 0.04 | 0.12 ± 0.01 |
| P117G/H124L‖ | 200 ± 41 | −0.016 ± 0.002 | 13.5 ± 0.2 | 0.26 ± 0.003 | 2.4 ± 0.1 | 0.153 ± 0.003 | — | — |
Values listed are at zero denaturant.
†Unfold at pH 2.2, measure folding at pH 5.3, 15°C, 0.1 M sodium acetate (27).
‡Unfold at pH 2.0, measure folding at pH 6.0, 20°C, 0.1 M sodium cacodylate, 2 mM EGTA (12). “%” denotes relative amplitudes.
§Unfold at pH 2.0, measure folding at pH 5.2, 15°C, 0.1 M sodium acetate (26). WT* is SNase P47G/P117G/H124L.
¶This work. Same conditions as †.
‖This work. Unfold at pH 2.2, measure folding at pH 8.5, 50 mM CHES, 20°C, 0.1 M NaCl.