Table 1.
Folding and unfolding kinetics of the selected AKBSUB mutants
| Protein | ΔGUnfold(H2O) (kJ/mol) | kF(H2O) (s−1) | kU(H2O) (s−1) | βT |
|---|---|---|---|---|
| AKBSUB | 14 ± 1 | 0.030 ± 0.002 | 8.01 × 10−5 ± 0.5 × 10−5 | 0.45∗ |
| AKBSUB Q199R | 16 ± 1 | 0.015 ± 0.003 | 1.50 × 10−5 ± 0.2 × 10−5 | 0.25∗ |
| AKBSUB Q199R/G213E | 21 ± 1 | 0.13 ± 0.01 | 1.70 × 10−5 ± 0.2 × 10−5 | 0.53 |
| AKBSUB Q199R/T179I | 24 ± 1 | 0.80 ± 0.04 | 2.0 × 10−5 ± 0.3 × 10−5 | 0.58 |
| AKBSUB Q199R/G214R | 25 ± 1 | 0.20 ± 0.02 | 3.0 × 10−6 ± 0.1 × 10−6 | 0.48 |
| AKBSUB Q199R/A193V | 26 ± 1 | 12.2 ± 0.2 | 1.5 × 10−4 ± 0.3 × 10−4 | 0.78 |
| AKBSUB Q199R/Q16L | 28 ± 1 | 0.70 ± 0.04 | 4.40 × 10−6 ± 0.7 × 10−6 | 0.57 |
ΔGUnfold (H2O) values are based on the equilibrium data (Fig. 2a), and kF(H2O) and kU(H2O) values are folding and unfolding rate constants extrapolated to 0 M GuHCl (Fig. 2b). βT (a measure of nativeness/compaction in the transition state for folding) was calculated as mf/(meq) where meq = mf + mu such that mf is the slope of the folding arm and mu is the slope of the unfolding arm in the Chevron plot (Fig. 2b).
∗
Taken from Couñago et al. (20).