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. Author manuscript; available in PMC: 2021 Jul 18.
Published in final edited form as: Nat Microbiol. 2021 Jan 18;6(3):392–400. doi: 10.1038/s41564-020-00844-1

Extended Data Fig. 3. Sample ITC results.

Extended Data Fig. 3

ITC data for suramin binding to each VSG protein. The upper panels contain the baseline corrected raw data, and the lower panel contains the peak-integrated, concentration normalized data for the heat of reaction vs. molar ratio of suramin per VSG protein. (a) VSGSur was measured 3 times, independently: 300μM suramin was titrated into 46μM VSGsur, the curve fitted with a single binding site model to calculate a Kd of 234+/- 28 nM and N of 0.49 +/- 0.03 (b) VSGSur H122A was measured 3 times, independently: 450μM suramin was titrated into 51.1μM VSGSur H122A. A Kd could not be fit to the data, although it is clear that the mutation negatively affected the binding affinity. (c) VSGSur N130A was measured 2 times, independently: 300μM suramin was titrated into 40μM VSGSur N130A. No binding was detected. (d) VSG2 was measured 2 times, independently: 200μM Suramin was titrated into 20μM VSG2 protein. No binding was detected. (e) VSG3 was measured 2 times, independently: 300μM suramin was titrated into 53.1μM VSG3. No binding was detected. (f) VSG13 was measured 2 times, independently: 200μM Suramin was titrated into 20μM VSG132 protein. No binding was detected.