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In a structural analysis of the proteasome activator PafE in Mycobacteriumtuberculosis, the binding of the activator or shorter constructs to the 20Sproteasome core particle (20S CP) or derivatives was measured by isothermaltitration calorimetry (Bai et al. Proc Natl Acad Sci USA 113: E1983-E1992.2016). The data were fitted by the authors by nonlinear least squares to givecurvilinear profiles that, at least in part, appear to fit the data very well.However, reanalysis of the data shows that the profiles are much better (P <0.001) represented as multiphasic, i.e. by a series of straight lines separatedby discontinuous transitions, often in the form jumps, than by the conventionalcurvilinear profiles.

'Perfectly' curvilinear profiles for binding as determined by ITC may in fact be multiphasic