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Glycoconj J ; 13(4): 599-607, 1996 Aug.
Article in English | MEDLINE | ID: mdl-8872117

ABSTRACT

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.


Subject(s)
Carbohydrates/chemistry , Glycopeptides/chemistry , Proteins/chemistry , Proteoglycans/chemistry , Magnetic Resonance Spectroscopy , Protein Structure, Secondary , Protons , Vesicular Transport Proteins
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