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. Author manuscript; available in PMC: 2021 Oct 6.
Published in final edited form as: Biochemistry. 2020 Mar 31;59(39):3696–3708. doi: 10.1021/acs.biochem.0c00035

Figure 2.

Figure 2.

Replicate isothermal calorimetry assays showing WDR5 interacts with specifically with H3R2. a. Histone H3 1–12aa peptide sequence with R to K mutant positions underlined b. Raw power differentials (DP) of peptide titrations c. Integrated heats of binding; error bars represent the standard error between two replicate titrations d. Dissociation constants for replicate titrations determined by fitting heat integrations to a one-site binding model e. Histogram of thermodynamic parameters for interacting peptides (ΔG, Gibbs free energy change; ΔH, enthalpy change; T, temperature in Kelvin; ΔS, entropy change) f. Tabulated thermodynamic parameters for interacting peptides (n.d., not detected). Peptides bound WDR5 with stoichiometries (N-values) between 0.9 and 1.1.