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. 2016 Nov 3;6:36346. doi: 10.1038/srep36346

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.