1H NMR studies of hydroxy protons of the V[β-Gal(1→3)-α-GalNAc(1→O)]THPGY glycopeptide
| ISSN: | 0008-6215 |
|---|---|
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88634c635df2e97daac79222fdeb5d44 https://doi.org/10.1016/s0008-6215(01)00271-3 |
| Rights: | CLOSED |
| Přírůstkové číslo: | edsair.doi.dedup.....88634c635df2e97daac79222fdeb5d44 |
| Autor: | Thomas Norberg, Corine Sandström, Lennart Kenne, Lill Kindahl |
| Rok vydání: | 2001 |
| Předmět: |
Steric effects
Magnetic Resonance Spectroscopy Stereochemistry Molecular Conformation Disaccharide Disaccharides Biochemistry Analytical Chemistry chemistry.chemical_compound Humans Moiety Organic chemistry Hydrogen bond Chemical shift Organic Chemistry Glycopeptides Temperature Water General Medicine Nuclear magnetic resonance spectroscopy Peptide Fragments Glycopeptide Fibronectins chemistry Proton NMR Protons |
| Zdroj: | Carbohydrate Research. 336:319-323 |
| ISSN: | 0008-6215 |
| Popis: | The hydroxy protons of the disaccharide moiety in the glycopeptide Val-[beta-Gal(1-->3)-alpha-GalNAc(1-->O)]-Thr-His-Pro-Gly-Tyr (1) have been investigated in aqueous solution using (1)H NMR spectroscopy. The chemical shifts (delta), coupling constants ((3)J(CH,OH)), temperature coefficients (d delta/dT), exchange rates (k(ex)), and NOEs have been measured. The data show that the O(2')H of Gal has a reduced contact with water due to steric interference caused by the 2-acetamido group of GalNAc. No interaction, in terms of hydrogen bonding exists between the disaccharide and the peptide moieties, but the rotation around the sugar-peptide linkage is restricted. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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