title: Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding.
abstract: 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.
authors.affiliation: Systems Biophysics and Functional Nanosystems, Ludwig-Maximilians-Universität München, Amalienstrasse 54, 80799 Munich, Germany.
authors.forename: Susanne A I
authors.initials: SA
authors.lastname: Seidel
authors.forename: Christoph J
authors.initials: CJ
authors.lastname: Wienken
authors.forename: Sandra
authors.initials: S
authors.lastname: Geissler
authors.forename: Moran
authors.initials: M
authors.lastname: Jerabek-Willemsen
authors.forename: Stefan
authors.initials: S
authors.lastname: Duhr
authors.forename: Alwin
authors.initials: A
authors.lastname: Reiter
authors.forename: Dirk
authors.initials: D
authors.lastname: Trauner
authors.forename: Dieter
authors.initials: D
authors.lastname: Braun
authors.forename: Philipp
authors.initials: P
authors.lastname: Baaske
mesh_terms: D001665:Binding Sites; D008024:Ligands; D044085:Microfluidics / Q000379:methods*; D011485:Protein Binding; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011506:Proteins