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Literature DB >> 8872117

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

E V Curto¹, T T Sakai, M J Jablonsky, S Rio-Anneheim, J C Jacquinet, N R Krishna.

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.

Entities: Chemical

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Year: 1996 PMID： 8872117 DOI： 10.1007/bf00731448

Source DB: PubMed Journal: Glycoconj J ISSN： 0282-0080 Impact factor: 2.916

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References

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

Review 1. Proteoglycans: structures and interactions.

2. A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure.

3. NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.

4. Solution structure of trypsin modulating oostatic factor is a left-handed helix.

5. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins.

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