Fig. 2: ITC analysis of the IKKα and IKKβ interactions with IκBα pep.
From: Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates
a Sequences of the IκBα pep wt and C308L synthetic peptides. b, c Representative ITC binding isotherms for the indicated interactions. The experiments used purified IKKα(10-667) EE or IKKβ(1-669) EE proteins at concentrations between 22 and 50 μM, depending on the experiment, and peptide concentrations were adjusted accordingly (i.e. between 220 and 975 μM). DP: differential power. The data were analyzed by global fitting (see Table 1). The residuals are calculated as differences between fitted and experimental values, whereas the error bars correspond to the root-mean-square-deviation (RMSD) of the fitted and measured injection data as implemented in SEDPHAT61. Each interaction was measured in at least two independent ITC titration experiments. Source data are provided as a Source Data file.
