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920 MHz ultra-high field NMR approaches to structural glycobiology
Authors:Koichi Kato  Hiroaki Sasakawa  Yukiko Kamiya  Maho Utsumi  Michiko Nakano  Noriko Takahashi  Yoshiki Yamaguchi
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
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.
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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