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. Author manuscript; available in PMC: 2015 Dec 24.
Published in final edited form as: Nature. 2006 May 21;442(7098):91–95. doi: 10.1038/nature04802

Figure 1. NMR, calorimetry and surface plasmon resonance-based studies of the binding of the BPTF PHD finger by H3(1–15)K4 peptides as a function of methylation state.

Figure 1

a, Sequences of the PHD finger of human BPTF and histone H3(1–20). b, Left panel: superposition of 1H,15N-HSQC NMR spectra showing BPTF PHD finger amide resonances in the absence (black) and presence (red) of 5 equivalents of H3(1–15)K4me3 peptide. Right panel: plots of chemical shift changes of the Y17 amide resonance of the BPTF PHD domain as a function of peptide concentration for different methylation states of H3K4. c, Isothermal titration calorimetry enthalpy plots for the binding of the BPTF PHD finger by H3(1–15)K4me3 (left panel) and H3(1–15)K4me2 (right panel) peptides. d, Surface plasmon resonance-based binding curves for the BPTF PHD finger with biotin-labelled H3(1–20) peptides as a function of K4 methylation state.