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• W2032012179 abstract "Partial assignments for the 1H-NMR resonances of the aromatic residues in human interleukin 6 (IL-6) are reported. The homonuclear Hartmann-Hahn spectrum clearly shows all connectivities for the histidine, tyrosine and tryptophan residues that exist in IL-6. Using a deuterium exchange method, the imidazole proton resonances of His-16 and His-165 have been assigned. Iodination of the tyrosine residues led to the assignment of Tyr-32. Photo-chemically induced dynamic nuclear polarization data have shown that His-16, Tyr-32 and Trp-158 are exposed to solvent, whereas His-165, Tyr-98 and Tyr-101 are buried. Iodination of Tyr-32 gave no significant effect on IL-6 activity, suggesting that Tyr-32 is not responsible for IL-6 activity." @default.
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• W2032012179 date "1990-12-01" @default.
• W2032012179 modified "2023-09-24" @default.
• W2032012179 title "Proton nuclear magnetic resonance study of human interleukin 6: Chemical modifications and partial spectral assignments for the aromatic residues" @default.
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• W2032012179 doi "https://doi.org/10.1016/0167-4838(90)90278-n" @default.
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