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

From National Research Council Canada

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Subject1H; 1H-NMR; anomeric; assignment; chemical; chemical shift; coupling; disaccharide; glcnac; glucans; glycopeptide; 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
Abstract
The 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
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  • J.Biol.Chem. 257, no. 19 (10 October 1982): 11207–11209.
LanguageEnglish
NRC numberBRISSON1982
NPARC number9371704
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