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Frontispiece: Mixed Fluorotryptophan Substitutions at the Same Residue Expand the Versatility of 19 F Protein NMR Spectroscopy
Author(s) -
Kenward Calem,
Shin Kyungsoo,
Rainey Jan K.
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201881464
Subject(s) - nuclear magnetic resonance spectroscopy , residue (chemistry) , chemistry , spectroscopy , peptide , fluorine 19 nmr , crystallography , stereochemistry , biochemistry , physics , quantum mechanics
19 F NMR spectroscopy of protein isoform mixtures containing assorted combinations of fluorotryptophan isomers at each Trp was employed to compare the binding of two peptide ligands to a 19 F‐labeled G‐protein‐coupled receptor fragment in micellar solution. Protein mixtures with assorted flurotryptophan labels are straightforward to produce and study, providing a sensitive means to deconvolute site‐specific behavior and follow otherwise obscure perturbations in a wide range of protein systems. More information can be found in the Communication by J. K. Rainey et al. on page 3391 ff.