Related Experiment Video
Updated: Aug 11, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Tuning the conformation properties of a peptide by glycosylation and phosphorylation
Fu-Cheng Liang1, Rita P-Y Chen, Chun-Cheng Lin
1Institute of Chemistry, Academia Sinica, Taipei, Taiwan, ROC.
Abstract:
We have deployed the alpha-helical hairpin peptide (alpha-helix/turn/alpha-helix) and used it as a model system to explore how glycosylation and phosphorylation might affect the conformational properties of the peptide. The native conformations of the modified peptides in buffer solution have been compared with that of the wild-type peptide by nuclear magnetic resonance spectroscopy. Circular dichroism spectroscopy was used to probe the effects of an O-linked beta-GlcNAc and a phosphate group on the overall folding stability of the peptide. Finally, the rate of fibrillogenesis was used to infer the effects of these chemical modifications on the alpha-to-beta transition as well as the rate of nucleation of amyloidogenesis.
Related Concept Videos
Protein Glycosylation
Glycosylation occurs in...
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Protein Folding Quality Check in the RER
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
