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. Author manuscript; available in PMC: 2017 Apr 19.
Published in final edited form as: ChemMedChem. 2015 Nov 23;11(8):919–927. doi: 10.1002/cmdc.201500441

Figure 2. Binding data for compound 2.

Figure 2

A) NMR titration of compound 2 binding to YopH-NT (50 μM) using 2D [1H,15N] HSQC spectra. The black contours represent the spectrum for the free protein, while the spectra in cyan, red, yellow, green, purple, blue and fuchsia, respectively, represent YopH-NT in presence of increasing amounts of compound 2 (20 μM, 40 μM, 60 μM, 100 μM, 150 μM, 200 μM and 250 μM, respectively). B) Kd determination for compound 2 using chemical shift perturbation titrations; Kd = 17.3 μM. C) Isothermal titration calorimetry data for the binding between compound 2 and YopH-NT (Kd = 6.6 μM, ΔH =−9.8 Kcal/mol, −TΔS = 2.7 Kcal/mole, n = 0.67).