Virtual coupling in the 1H NMR spectrum of N,N'-diacetyl chitobioside. Application to glycopeptides: J.Biol.Chem.

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TypeArticle
Journal titleJ.Biol.Chem.
Volume257
Issue19
Pages1120711209; # of pages: 3
Subject1H; 1H-NMR; analysis; ANOMERIC; assignment; chemical; chemical shift; COUPLING; DISACCHARIDE; Disaccharides; GlcNAc; GLUCANS; glycopeptide; Glycopeptides; Hydrogen; long range; Magnetic Resonance Spectroscopy; Mannose; N-linked; NMR; NMR-SPECTRA; Protein Binding; RESONANCE; SPECTRA; structure; Structure-Activity Relationship; Support,Non-U.S.Gov't; Temperature; Virtual
AbstractThe unexplained line shape for the anomeric hydrogen resonance of the core GlcNAc observed in the 1H NMR spectra of high mannose N-linked glycopeptides (Bruch, R. C., and Bruch, M. D. (1982) J. Biol. Chem. 257, 3409-3413) can be accounted for by virtual coupling. Complete assignment, at various temperatures, of the 360-MHz 1H NMR spectrum of beta-methyl N,N'-diacetyl chitobioside confirms this interpretation. This analysis has revealed the existence of a long range chemical shift perturbation in these glycopeptides which is interpreted as arising from their specific three-dimensional structure
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberBRISSON1982
NPARC number9371704
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Record identifier445e7da9-f26a-4fdf-ae47-94d9b3154da0
Record created2009-07-10
Record modified2016-05-09
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