Figure 3.

Interaction between Ref‐Cys367Ser and hYAP^51–99/hTAZ^14–56. A, B. Representative thermograms obtained in the FTDA with Ref‐Cys367Ser (1–2 µM) in the absence or presence of hYAP^51–99 (A) or hTAZ^14–56 (B) (20 µM). The melting temperatures (T _m) were obtained by plotting the first derivative of the fluorescence emission (F) as a function of the temperature (–dF/dT). The curve minimum corresponds to T _m. The arrow shows the thermal shift (ΔT _m) observed upon peptide binding. The indicated T _m have been measured for the experiments depicted on the figure. These T _m are slightly different from the T _m presented on Table II because these later are the average values obtained from several independent measurements. Upper panels: Representative sensorgrams obtained with Ref‐Cys367Ser immobilized on the chips and different concentrations of hYAP^51–99 (C) hTAZ^14–56 (D). Lower panels: R_eq vs [YAP^60–100/TAZ^17–56] plots. R_eq are the responses measured at equilibrium (plateau values in the above sensorgrams). These curves were fitted with 1 site binding equation model to determine K _d.