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Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding.
- Source :
-
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2012 Oct 15; Vol. 51 (42), pp. 10656-9. Date of Electronic Publication: 2012 Sep 24. - Publication Year :
- 2012
-
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.<br /> (Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Details
- Language :
- English
- ISSN :
- 1521-3773
- Volume :
- 51
- Issue :
- 42
- Database :
- MEDLINE
- Journal :
- Angewandte Chemie (International ed. in English)
- Publication Type :
- Academic Journal
- Accession number :
- 23001866
- Full Text :
- https://doi.org/10.1002/anie.201204268