Selective Incorporation of  19 F‐Labeled Trp Side Chains for NMR‐Spectroscopy‐Based Ligand–Protein Interaction Studies | Zendy

Leone Marilisa | Zendy; RodriguezMias Ricard A. | Zendy; Pellecchia Maurizio | Zendy

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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.

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