Premium
Label‐Free Microscale Thermophoresis Discriminates Sites and Affinity of Protein–Ligand Binding
Author(s) -
Seidel Susanne A. I.,
Wienken Christoph J.,
Geissler Sandra,
JerabekWillemsen Moran,
Duhr Stefan,
Reiter Alwin,
Trauner Dirk,
Braun Dieter,
Baaske Philipp
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201204268
Subject(s) - microscale thermophoresis , affinities , chemistry , microscale chemistry , biophysics , ligand (biochemistry) , thermophoresis , membrane , binding site , plasma protein binding , aptamer , biochemistry , receptor , nanotechnology , biology , microbiology and biotechnology , materials science , nanofluid , mathematics education , mathematics , nanoparticle
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.