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Yamaguchi, Yoshiki

doi:10.4052/tigg.20.117

Cited by 10 publications

(8 citation statements)

References 76 publications

(37 reference statements)

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“…Although, upon an increase of pH, the carbonyl 13 C peaks coalesce because of increased exchange rates, the 13 C resonance of the GlcNAc-2 acetamide group still exhibited a doublet peak. This is consistent with the data obtained via saturation transfer experiments following irradiation of the water resonance [85]. These NMR data demonstrate that the degree of protection of the amide protons is different for the different GlcNAc amide groups of the Fc glycan.…”

Section: Local Structures and Dynamics Of Glycanssupporting

confidence: 90%

“…The intra-molecular carbohydrate-protein interactions were characterized by observing NOE connectivities between the sugar and amino acid residues, which is consistent with the crystal structures even in the absence of the terminal Gal residues (Fig. 10) [85]. All these NMR data indicate that the glycans are not flipped out into the solvent but buried between the two C H 2 domains even in the agalactosyl form highly populated in rheumatoid arthritis.…”

Section: Agalactosylation Of the Fc Glycansmentioning

confidence: 66%

“…The stable-isotope-assisted NMR methods thus developed for IgG-Fc as a model system provide a general strategy for structural glycobiology. For example, it has been demonstrated that a series of glycopeptides cleaved from the metabolically 13 C/ 15 N-labeled IgG glycoprotein can be useful tools for detailed NMR analyses for the characterization of sugar-binding modes of lectins [61,85,94]. Applicability of the stable-isotope-labeling methods of glycans is not limited to the field of NMR studies.…”

Section: Discussionmentioning

confidence: 99%

“…15 N relaxation analyses of these groups demonstrated that the acetamide group of GlcNAc-5, which is located at the non-reducing terminal of the Mana1-3 branch, is significantly mobile in comparison with those of other GlcNAc residues [85].…”

Section: Local Structures and Dynamics Of Glycansmentioning

confidence: 99%

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Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system

Kato

Yamaguchi

Arata³

2010

Progress in Nuclear Magnetic Resonance Spectroscopy

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Section: Local Structures and Dynamics Of Glycanssupporting

confidence: 90%

Section: Agalactosylation Of the Fc Glycansmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Section: Local Structures and Dynamics Of Glycansmentioning

confidence: 99%

See 2 more Smart Citations

Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system

Kato

Yamaguchi

Arata³

2010

Progress in Nuclear Magnetic Resonance Spectroscopy

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“…To date, glycoprotein structures have been solved by X-ray crystallographic analysis as well as NMR spectroscopy methods. [19] Glycosylation occurs at sites such as loops, helices and b-sheets. Full-length oligosaccharides are known to exhibit dynamic conformational ensembles that appear to widely fluctuate.…”

Section: Introductionmentioning

confidence: 99%

Homogeneous Human Complex‐Type Oligosaccharides in Correctly Folded Intact Glycoproteins: Evaluation of Oligosaccharide Influence On Protein Folding, Stability, and Conformational Properties

Kajihara

Tanabe

Sasaoka

et al. 2012

Chemistry A European J

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The N-glycosylation of proteins is generated at the consensus sequence NXS/T (where X is any amino acid except proline) by the biosynthetic process, and occurs in the endoplasmic reticulum and Golgi apparatus. In order to investigate the influence of human complex-type oligosaccharides on counterpart protein conformation, crambin and ovomucoide, which consist of 46 and 56 amino acid residues, respectively, were selected for synthesis of model glycoproteins. These small glycoproteins were intentionally designed to be glycosylated at the α-helix (crambin: 8 position), β-sheet (crambin: 2 position) and loop position between the antiparallel β-sheets (ovomucoide: 28 position), and were synthesized by using a peptide-segment coupling strategy. After preparation of these glycosylated polypeptide chains, protein folding experiments were performed under redox conditions by using cysteine-cystine. Although the small glycoproteins bearing intentional glycosylation at the α-helix and β-sheet exhibited a suitable folding process, glycosylation at the loop position between the antiparallel β-strands caused multiple products. The conformational differences in the isolated homogeneous glycoproteins compared with non-glycosylated counterparts were evaluated by circular dichroism (CD) and NMR spectroscopy. These analyses suggested that this intentional N-glycosylation did not result in large conformational changes in the purified protein structures, including the case of glycosylation at the loop position between the antiparallel β-strands. In addition to these experiments, the conformational properties of three glycoproteins were evaluated by CD spectroscopy under different temperatures. The oligosaccharides on the protein surface fluctuated considerably; this was dependent on the increase in the solution temperature and was thought to disrupt the protein tertiary structure. Based on the measurement of the CD spectra, however, the glycoproteins bearing three disulfide bonds did not exhibit any change in their protein tertiary structure. These results suggest that the oligosaccharide conformational fluctuations were not disruptive to protein tertiary structure, and the tertiary structure of glycoproteins might be stabilized by the disulfide bond network.

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Glycoproteins and Antibodies: Solution NMR Studies

Kato

Yamaguchi

2011

Encyclopedia of Magnetic Resonance

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Untitled

Cited by 10 publications

References 76 publications

Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system

Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system

Homogeneous Human Complex‐Type Oligosaccharides in Correctly Folded Intact Glycoproteins: Evaluation of Oligosaccharide Influence On Protein Folding, Stability, and Conformational Properties

Glycoproteins and Antibodies: Solution NMR Studies

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