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Selective Incorporation of 19 F‐Labeled Trp Side Chains for NMR‐Spectroscopy‐Based Ligand–Protein Interaction Studies
Author(s) -
Leone Marilisa,
RodriguezMias Ricard A.,
Pellecchia Maurizio
Publication year - 2003
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300597
Subject(s) - side chain , chemistry , nuclear magnetic resonance spectroscopy , tryptophan , ligand (biochemistry) , isotopic labeling , fluorine 19 nmr , nuclear magnetic resonance spectroscopy of nucleic acids , protein structure , stereochemistry , tyrosine , histidine , protein data bank (rcsb pdb) , amino acid , biochemistry , transverse relaxation optimized spectroscopy , organic chemistry , receptor , polymer
F marks the spot : We report a new technique for selectively labeling Trp side chains in proteins with 19 F by using 3 β ‐indoleacrilic acid as an inhibitor of tryptophan biosynthesis. Our method finds useful application in the study of protein–protein or protein–ligand interactions (see figure) by means of 19 F NMR spectroscopy.