Intramolecular N‑Glycan/Polypeptide Interactions Observed at Multiple N‑Glycan Remodeling Steps through [13C,15N]‑N‑Acetylglucosamine Labeling of Immunoglobulin G1

Asparagine-linked (N) glycosylation is a common eukaryotic protein modification that affects protein folding, function, and stability through intramolecular interactions between N-glycan and polypeptide residues. Attempts to characterize the structure–activity relationship of each N-glycan are hinde...

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Veröffentlicht in:	Biochemistry (Easton) 2015-01, Vol.54 (2), p.313-322
1. Verfasser:	Barb, Adam W
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylglucosamine - chemistry Carbohydrate Sequence glucose glutamine glycoproteins Glycoproteins - chemistry Glycoproteins - metabolism Glycosylation glycosyltransferases Glycosyltransferases - metabolism HEK293 Cells Humans immunoglobulin G Immunoglobulin G - chemistry Immunoglobulin G - metabolism mannose mass spectrometry Models, Molecular Molecular Sequence Data nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular Peptides - chemistry Peptides - metabolism polypeptides Polysaccharides - chemistry Polysaccharides - metabolism protein folding Recombinant Proteins - metabolism stable isotopes structure-activity relationships uridine diphosphate
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