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Thermodynamic properties of GCA, TCA, and TCDCA binding to norovirus P domains. Titrations were performed at 25°C by injecting consecutive aliquots of 300 μM bile acids into 30 to 35 μM GII.1 or GII.10 P domains. All binding reactions were exothermic. The ITC data showed that GII.1 (A) and GII.10 (B) domains bound various types of bile acid with similar affinities. Thermodynamic constants (ΔH, ΔS, and Kd) are summarized in Table 1.
