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. 2019 Aug 9;28(10):1750–1757. doi: 10.1002/pro.3694

Figure 1.

Figure 1

Isothermal titration calorimetry titrations of l‐methionine and d‐methionine binding to MetQ variants. ITC titrations of (a) the binding of l‐methionine to wild‐type MetQ; (b) the binding of d‐methionine to wild‐type MetQ; (c) displacement ITC titration of the binding of l‐methionine to wild‐type MetQ in the presence of d‐methionine; (d) the binding of l‐methionine to substrate‐free N238A Neisseria meningitides MetQ; (e) the binding of d‐methionine to N238A MetQ. The derived dissociation constants and enthalpies are presented in Table 1. Protein concentrations of MetQ ([MetQ]), l‐methionine ([l‐met]), and d‐methionine ([d‐met]) are shown in the figures. ITC, isothermal titration calorimetry