Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding.
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ABSTRACT:
SUBMITTER: Seidel SA
PROVIDER: S-EPMC3588113 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Publications
Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding.
Seidel Susanne A I SA Wienken Christoph J CJ Geissler Sandra S Jerabek-Willemsen Moran M Duhr Stefan S Reiter Alwin A Trauner Dirk D Braun Dieter D Baaske Philipp P
Angewandte Chemie (International ed. in English) 20120924 42
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 Ca(2+) ions to synaptotagmin was quantified. ...[more]
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