Novel forms of protein glycosylation
Related Experiment Video
Updated: Oct 27, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
1Department of Bio-organic Chemistry, Bijvoet Center, Utrecht University, The Netherlands. vlieg@accu.uu.nl
Abstract:
A large number of new glycans, derived from glycoproteins, has been characterized in the past few years. O-linked fucose was found in epidermal growth factor-like domains of several proteins. For the N-linked glycans of Helix pomatia hemocyanin, novel types of antennae were identified. The positions of noncarbohydrate substituents were established in N-glycans. C-mannosylation of a tryptophan residue was discovered in human ribonuclease 2 and is the first example of C-glycosylation in glycoproteins.
More Related Videos
Related Concept Videos
Protein Glycosylation
Glycosylation occurs in...
Proteoglycans
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Folding Quality Check in the RER
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Matrix Proteoglycans and Glycoproteins

