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The strategy of applying fluorine NMR to characterize ligand binding to a membrane protein prepared with mixtures of tryptophans substituted with F at different positions on the indole ring was tested. The 19F NMR behavior of 4‐, 5‐, 6‐, and 7‐fluorotryptophan were directly compared as a function of both micellar environment and fragment size for two overlapping apelin receptor (AR/APJ) segments;...
19F 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 19F‐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...
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