Label-Free Microscale Thermophoresis Discriminates Sites and Affinity of Protein–Ligand Binding

Angewandte Chemie, 2012, DOI: 10.1002/anie.201204268, Issue 42, pages 10656–10659 published on 24.09.2012

Angewandte Chemie, online article

Look, no label! Microscale thermophoresis makes use of the intrinsic fluorescence of proteins to quantify the binding affinities of ligands and discriminate between binding sites. This method is suitable for studying binding interactions of very small amounts of protein in solution. The binding of ligands to iGluR membrane receptors, small-molecule inhibitorss to kinase p38, aptamers to thrombin, and Ca2+ ions to synaptotagmin was quantified.  

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