Thread: NMR paper Complete 1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein
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Default Complete 1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein
Complete 1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins.

Related Articles Complete 1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins.

Glycoconj J. 1996 Aug;13(4):599-607

Authors: Curto EV, Sakai TT, Jablonsky MJ, Rio-Anneheim S, Jacquinet JC, Krishna NR

We present complete 1H NMR assignments for two synthetic glycopeptides representative of the carbohydrate-protein 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)-G ly. 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.

PMID: 8872117 [PubMed - indexed for MEDLINE]



Source: PubMed
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