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. 2010 May 11;107(21):9567–9571. doi: 10.1073/pnas.1001541107

Fig. 2.

Fig. 2.

Biochemical characterization of the selected KD variants. (A, B) Analyses of the binding specificity of the KD variants (1 μM) isolated against DR4 (KD413 and KD415) and DR5 (KD506 and KD548) (A), or TNFα (KDT26) (B), which were determined by ELISA. PgnKD2 (1 μM), TRAIL (0.1 μM), and the anti-TNFα mAb infliximab (0.1 μM) were used as controls. Binding specificities for the other KD variants are shown in Table S1. (C) Far-UV CD spectra of PgnKD2 and the KD variants (100 μg/mL in PBS, pH 7.4) to monitor the secondary structure are shown. (D) DSC thermograms of PgnKD2 and the selected KD variants. The change in heat capacity at constant pressure (ΔCp) was plotted against the temperature. The temperature of maximum heat capacity (Tm) for each sample was indicated in the panel.