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Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
Author(s) -
Mayer Moriz,
Meyer Bernd
Publication year - 1999
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/(sici)1521-3773(19990614)38:12<1784::aid-anie1784>3.0.co;2-q
Subject(s) - saturation (graph theory) , chemistry , molecule , ligand (biochemistry) , nuclear magnetic resonance spectroscopy , computational chemistry , analytical chemistry (journal) , crystallography , stereochemistry , chromatography , biochemistry , organic chemistry , receptor , mathematics , combinatorics
Fast identification of binding activity directly from mixtures of potential ligands is possible with the NMR method described, which is based on saturation transfer to molecules in direct contact to a protein. In addition, the ligand's binding epitope is easily identified. High sensitivity and ease of use are the principal advantages of this method. The picture shows the normal 1D NMR spectrum of a mixture and the spectrum obtained by applying the STD method, which exclusively shows signals from molecules with binding affinity.