| Literature DB >> 29711196 |
Abstract
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. © 1999 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.Entities:
Keywords: Bioaffinity studies; Combinatorial chemistry; Molecular recognition; NMR spectroscopy
Year: 1999 PMID: 29711196 DOI: 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0.CO;2-Q
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336