920 MHz ultra-high field NMR approaches to structural glycobiology |
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Authors: | Koichi Kato Hiroaki Sasakawa Yukiko Kamiya Maho Utsumi Michiko Nakano Noriko Takahashi Yoshiki Yamaguchi |
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Affiliation: | 1. Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan;2. Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan;3. GLYENCE Co., Ltd., 406 Nagoya Life Science Incubator, 2-22-8 Chikusa, Chikusa-ku, Nagoya 474-0858, Japan;4. Genomic Sciences Center, RIKEN Yokohama Institute, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan;5. The Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan;6. Structural Glycobiology Laboratory, Systems Glycobiology Research Group, RIKEN Frontier Research System, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan |
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Abstract: | Although NMR spectroscopy has great potential to provide us with detailed structural information on oligosaccharides and glycoconjugates, the carbohydrate NMR analyses have been hampered by the severe spectral overlapping and the insufficiency of the conformational restraints. Recently, ultra-high field NMR spectrometers have become available for applications to structural analyses of biological macromolecules. Here we demonstrate that ultra-high fields offer not only increases in sensitivity and chemical shift dispersion but also potential benefits for providing unique information on chemical exchange and relaxation, by displaying NMR spectral data of oligosaccharide, glycoprotein, and glycolipid systems recorded at a 21.6 T magnetic field (corresponding to 920 MHz 1H observation frequency). The ultra-high field NMR spectroscopy combined with sugar library and stable-isotope labeling approaches will open new horizons in structural glycobiology. |
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Keywords: | Aβ, amyloid β protein 3D, three-dimensional CD, α-cyclodextrin CSA, chemical shift anisotropy HSQC, heteronuclear single-quantum correlation Ig, immunoglobulin NMR, nuclear magnetic resonance NOE, nuclear Overhauser effect PA, pyridylaminated RDC, residual dipolar coupling TROSY, transverse relaxation-optimized spectroscopy |
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