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Complete1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins

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Abstract

We present complete1H NMR assignments for two synthetic glycopeptides representative of the carbohydrateprotein linkage region of serglycin proteoglycans. The peptides are: Ser(Galp-Xylp)-Gly-Ser-Gly-Ser(Galp-Xylp)-Gly and, Ser(Galp-Xylp)-Gly-Ser(Galp-Xylp)-Gly-Ser(Galp-Xylp)-Gly. A number of 2D NMR spectra together with a 3D NOESY-TOCSY spectrum were acquired at 600 MHz to complete the assignments of the glycopeptides dissolved in water with 40% trifluoroethanol. Preliminary analysis of the NMR data suggests folded structures for the glycopeptides.

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Correspondence to N. Rama Krishna.

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Curto, E.V., Sakai, T.T., Jablonsky, M.J. et al. Complete1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins. Glycoconjugate J 13, 599–607 (1996). https://doi.org/10.1007/BF00731448

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Keywords

  • glycopeptide
  • NMR
  • proteoglycan
  • serglycin
  • secondary structure