Figure 4.

Association and dissociation curves of the SPR experiments. Most IFN-γ-Rx variants behave similarly as the wild-type (a) and mutant H222R (b): they bind IFN-γ-SC very fast but also release it fast. Two high-affinity binders, mutant N96W (c) and the double mutant N96W+H222R, bind the IFN-γ-SC molecules for a longer time, thus increasing the affinity to IFN-γ. The SPR experimental signal is in black; the fitted curves from which the association and dissociation kinetic constants are calculated are in red. The SPR data for all variants are in Table 3.