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. 2008 Feb 22;9(4):370–376. doi: 10.1038/embor.2008.11

Table 1.

Values of the dissociation constants between H3 peptides and AIRE–PHD1 wild type (WT) and mutants measured by fluorescence spectroscopy and isothermal titration calorimetry

AIRE–PHD1 Peptide KD (μM), fluorescence spectroscopy KD (μM), isothermal titration calorimetry
WT H3K4me0 4.7±0.8 6.5±0.2
WT H3K4me1 21.4±5.9 55.6±1.2
WT H3K4me2 >500 714±90
WT H3K4me3 ND NM
V301M H3K4me0 6.8±0.4 NM
C311Y H3K4me0 ND NM
D297A H3K4me0 173.0±18.6 146.8±6.1
D312A H3K4me0 ND ND
WT H3K4me0-R2A ND NM
D297A H3K4me3 ND NM
ND, not detectable, denotes binding too weak to be reliably quantified; NM, not measured.