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Michaelis-Menten binding curves of three aptamers are shown in Fig. 3A.
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Shown at the bottom right of Fig. 5a are schematic binding curves of four different protein kinases (for which the ligand has no affinity for one protein kinase).
Figure 1c shows titration binding curves for three tight SYNZIP interactions and one weak interaction.
We compared the binding curves for two preparations of β2GPI and for β2GPI-DV in the absence and in the presence of the dimerizing antibodies.
(f) Competition binding curves of Na+ ions for [125I]ET-1 [125I]ET-1 ETRs.
c The MST binding curves of KpBest L177T (red) to ATPγS.
Nevertheless, the binding curves of P2 and P3 clearly demonstrate the strong pH-dependence of Her2 binding (Fig. 4).
d The MST binding curve of KpBest A4 to ATPγS (red).
The binding curve of WT KpBest to ATPγS (black) is shown for comparison.
Critical helices potentially involved in channel activation are highlighted in the same colors as those in Fig. 7. b The MST binding curve of bBest2 to ATPγS.
(C ) ITC-derived binding curve of AnkR_AS titrated to AnkR_repeats.
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