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• W2034176824 endingPage "492" @default.
• W2034176824 startingPage "487" @default.
• W2034176824 abstract "The apoprotein corresponding to the mammalian photoreceptor rhodopsin has been expressed by using suspension cultures of HEK293S cells in defined media that contained 6- 15 N-lysine and 2- 13 C-glycine. Typical yields were 1.5–1.8 mg/liter. Incorporation of 6- 15 N-lysine was quantitative, whereas that of 2- 13 C-glycine was about 60%. The rhodopsin pigment formed by binding of 11- cis retinal was spectrally indistinguishable from native bovine rhodopsin. Magic angle spinning (MAS) NMR spectra of labeled rhodopsin were obtained after its incorporation into liposomes. The 15 N resonance corresponding to the protonated retinylidene Schiff base nitrogen was observed at 156.8 ppm in the MAS spectrum of 6- 15 N-lysine-labeled rhodopsin. This chemical shift corresponds to an effective Schiff base-counterion distance of greater than 4 Å, consistent with structural water in the binding site hydrogen bonded with the Schiff base nitrogen and the Glu-113 counterion. The present study demonstrates that structural studies of rhodopsin and other G protein-coupled receptors by using MAS NMR are feasible." @default.
• W2034176824 created "2016-06-24" @default.
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• W2034176824 date "1999-01-19" @default.
• W2034176824 modified "2023-10-16" @default.
• W2034176824 title "Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: Expression of ¹⁵ N-lysine- and ¹³ C-glycine-labeled opsin in a stable cell line" @default.
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• W2034176824 doi "https://doi.org/10.1073/pnas.96.2.487" @default.
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