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Complete1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins |
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| Authors: | Ernest V Curto Ted T Sakai Michael J Jablonsky Sandrine Rio-Anneheim Jean-Claude Jacquinet N Rama Krishna |
| Institution: | (1) Department of Biochemistry and Molecular Genetics, and Comprehensive Cancer Center, The University of Alabama at Birmingham, 35294-2041 Birmingham, AL, USA;(2) Laboratoire de Chimie des Sucres, U.R.A. 499, U.F.R. Faculté des Sciences, Université d'Orléans, B.P. 6759, F-45067 Orléans, France |
| 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.A preliminary account of this work was presented at an International Symposium held at the University of Alabama at Birmingham in November, 1994 on the occasion of the 65th birthday of Professor Lennart Rodén. |
| Keywords: | glycopeptide NMR proteoglycan serglycin secondary structure |
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