1990年12月
PROTON NUCLEAR-MAGNETIC-RESONANCE STUDY OF HUMAN INTERLEUKIN-6 - CHEMICAL MODIFICATIONS AND PARTIAL SPECTRAL ASSIGNMENTS FOR THE AROMATIC RESIDUES
BIOCHIMICA ET BIOPHYSICA ACTA
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- 巻
- 1041
- 号
- 3
- 開始ページ
- 243
- 終了ページ
- 249
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/0167-4838(90)90278-N
- 出版者・発行元
- ELSEVIER SCIENCE BV
Partial assignments for the H-1-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.
- リンク情報
- ID情報
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- DOI : 10.1016/0167-4838(90)90278-N
- ISSN : 0006-3002
- Web of Science ID : WOS:A1990EN91000004