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. 2016 Jun 9;291(32):16879–16891. doi: 10.1074/jbc.M116.728600

FIGURE 4.

FIGURE 4.

Binding of ubiquitin, phosphomimetic ubiquitin, and parkin UBL to the parkin core (parkin ΔUBL). A–C, isothermal titration calorimetry thermograms for ubiquitin (A), phosphomimetic ubiquitin (B), and parkin UBL (C) binding to parkin ΔUBL. Upper panels, raw data; lower panels, integrated heat values. D, dissociation constants determined from the ITC experiments. Phosphomimetic ubiquitin binds to the parkin core more avidly than wild-type ubiquitin (p < 0.001; Student's t test). E, thermodynamic parameters for the binding of ubiquitin, phosphomimetic ubiquitin, and the parkin UBL to parkin ΔUBL. Error bars indicate the S.E. in D and E of three independent experiments (n = 3).