Related Experiment Video

Updated: Oct 17, 2025

Mass Spectrometric Analysis of Glycosphingolipid Antigens
13:09

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Published on: April 16, 2013

16.8K

Nuclear Magnetic Resonance Methods in Structural Characterization of Glycosaminoglycans

Vitor H Pomin1, Barbara Mulloy2,3

  • 1Department of Biomolecular Sciences, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, Oxford, MS, USA.

Methods in Molecular Biology (Clifton, N.J.)
|October 9, 2021
PubMed

Keywords:
COSYGlycosaminoglycansHSQCNOESYTOCSY

More Related Videos

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition07:40

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

1.5K
Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining05:57

Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining

Published on: February 25, 2021

4.9K

Related Concept Videos

Glycosaminoglycans01:23

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
5.4K
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.1K
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
4.0K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.1K