Table 3 Summary of the thermodynamic-binding parameters for complex formation between H3 WT 10-mer peptide and mutant BAZ2A/B PHD

Titrations were performed at 25°C in triplicate, except where indicated, and values reported are the means ± s.e.m. Raw ITC data are shown for representative titrations in Supplementary Data (Supplementary Figure S2).

ProteinKD (µM)NΔH (kcal/mol)TΔS (kcal/mol)ΔG (kcal/mol)
BAZ2A PHD wt48 ± 21.29 ± 0.01−7.9 ± 0.1−2.0 ± 0.1−5.90 ± 0.02
BAZ2A PHD E1689Q83 ± 71.02 ± 0.03−9.6 ± 0.7−4.0 ± 0.8−5.57 ± 0.05
BAZ2A PHD E1689K*116 ± 61.1 ± 0.4−7.6 ± 2.5−2.2 ± 0.4−5.37 ± 0.03
BAZ2A PHD D1688N/E1689Q810 ± 501−9.0 ± 1.2−4.8 ± 1.2−4.22 ± 0.04
BAZ2B PHD wt47 ± 21.17 ± 0.02−8.3 ± 0.2−2.4 ± 0.2−5.90 ± 0.03
BAZ2B PHD E1944Q660 ± 601−8.5 ± 1.1−4.1 ± 1.1−4.34 ± 0.06
BAZ2B PHD E1944K>1000N.D.N.D.N.D.N.D.
  • * Titrations performed in duplicate.

  • N was fixed to 1 during the data fitting.