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. Author manuscript; available in PMC: 2006 Mar 31.
Published in final edited form as: J Biol Chem. 2005 Oct 31;280(51):41789–41792. doi: 10.1074/jbc.C500395200

Figure 2.

Figure 2

Fluorimetric binding equilibrium titrations of human CHD1 and H3K4 peptides. A. Graphic representation of the change in CHD1 intrinsic fluorescence upon peptide titrations, indicated as counts per minute (cpm). Binding reactions were performed in 25mM NaCl and 25mM Tris, pH 8.0. B. The fitted curve from the raw data presented in A used to calculate the dissociation constant of H3K4me3 binding to CHD1 is shown. C. The dissociation constants (Kd) for mono-, di-, and tri-methyl H3K4 peptides are indicated.