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ITC analysis of ligand binding.

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posted on 04.05.2012 by Jenni Leppiniemi, Toni Grönroos, Juha A. E. Määttä, Mark S. Johnson, Markku S. Kulomaa, Vesa P. Hytönen, Tomi T. Airenne

Thermograms of measurements performed at three different temperatures (A) 15°C, (B) 25°C and (C) 40°C are shown. At each temperature, core-bradavidin was first titrated with Brad-tag (1), followed by competitive titration with biotin (2). As a control measurement, core-bradavidin was titrated with biotin only (3). In order to prove that the intrinsic Brad-tag decreases the affinity towards biotin, wt bradavidin was also titrated with biotin (4). In addition, core-bradavidin was titrated with Brad-tag–EGFP at 15 and 25°C (5). (D) Comparison of the binding enthalpies of all measurements at different temperatures. Brad-tag had a clear effect on the binding enthalpy of the competitive titration with biotin at 15°C (endothermic Brad-tag binding) and 40°C (exothermic Brad-tag binding). At 25°C, the enthalpy of competitive titration was equal to that of titration with biotin only (no detectable binding of Brad-tag to core-bradavidin).

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