Table 1. Apparent formation constants (logK 12) of Zn(Hk)2 complexes of zinc hook peptides and their mutants at pH 7.4, I = 0.1 M, 25 °C.
Hook peptide | logK12 | Mutant peptide | logK12 |
---|---|---|---|
Hk4 | 14.93 ± 0.02 | Hk4VA | 14.41 ± 0.02 |
Hk5 | 15.37 ± 0.02 | Hk4PA | 14.19 ± 0.02 |
Hk6 | 16.44 ± 0.02 | Hk4PAVA | 13.96 ± 0.02 |
Hk8 | 17.78 ± 0.01 | Hk45LA | 19.06 ± 0.08 |
Hk10 | 18.64 ± 0.01 | Hk45VA | 19.78 ± 0.08 |
Hk12 | 19.02 ± 0.01 | Hk45LAVA | 17.89 ± 0.08 |
Hk14 | 19.19 ± 0.01 | ||
Hk23 | 19.49 ± 0.04 | Depsipeptide | logK12 |
Hk27 | 19.77 ± 0.04 | depsiHk8 | 15.33 ± 0.01 |
Hk31 | 20.47 ± 0.09 | depsiHk14 | 16.21 ± 0.01 |
Hk37 | 20.69 ± 0.06 | depsiHk14LA | 14.73 ± 0.03 |
Hk45 | 20.74 ± 0.06 | depsiHk14VALA | 13.97 ± 0.02 |
Values were calculated from cumulative protonation and stability constants determined potentiometrically (Tables S1 and S6) or determined spectropolarimetrically in competition experiments with zinc chelators (Fig. S4) and are not the results of ITC data fits.