AI Article Synopsis
- The study focuses on the structural properties of glycopeptides modeled after antifreeze glycoprotein (AFGP), a type of mucin-type glycoprotein.
- NMR measurements in different conditions showed that these glycopeptides create an intramolecular hydrogen bond that could influence the positioning of the sugar relative to the protein backbone.
- The research also examines the significance of the proline (Pro) residue's activity in AFGP.
Article Abstract
In order to investigate the structural properties of the sugar and peptide linkage region in glycoprotein, some glycopeptides were synthesized as a model for AFGP (antifreeze glycoprotein), which is one of the mucin-type glycoproteins. The results from n.m.r. measurements in DMSO and aqueous conditions revealed that the glycopeptides form an intramolecular hydrogen bond between the amide proton of N-acetylgalactosamine (GalNAc) and the carbonyl oxygen of threonine (Thr) to which the GalNAc is covalently linked. This intramolecular hydrogen bond may play an important role in determining the orientation of the sugar moiety relative to the protein backbone. The roles for the activity of the proline (Pro) residue in AFGP were also discussed.
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| http://dx.doi.org/10.1016/s0141-8130(05)80036-4 | DOI Listing |
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