Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

MALDI-TOF Mass Spectrometry

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

Mass Spectrometry: Complex Analysis

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Feature Down-Selection to Improve Supervised Classification by Machine Learning on Mass Spectrometry Imaging Data.

Molecules (Basel, Switzerland)·2026

Same author

Quantitative determination of longitudinal CNS cholesterol loss during myelin damage and repair.

bioRxiv : the preprint server for biology·2026

Same author

Lipidomics in Children: Noninvasive Sebum Sampling in Children and Adults Allows for Assessment of Lipidomic Differences According to Age, Sex, and Biological Relatedness.

Analytical chemistry·2026

Same author

Almost Nobody Is Using ChatGPT to Write Academic Science Papers (Yet).

Big data and cognitive computing·2025

Same author

Exploring Sample Storage Conditions for the Mass Spectrometric Analysis of Extracted Lipids from Latent Fingerprints.

Biomolecules·2025

Same author

Groomed Fingerprint Sebum Sampling: Reproducibility and Variability According to Anatomical Collection Region and Biological Sex.

Molecules (Basel, Switzerland)·2025

Search research articles

Related Experiment Video

Updated: Jun 24, 2026

Glycopeptide Capture for Cell Surface Proteomics

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 10, 2014

Glycopeptide analysis by mass spectrometry.

Dilusha S Dalpathado¹, Heather Desaire

¹Department of Chemistry, University of Kansas, Lawrence, KS 66045, USA.

|May 22, 2008

Summary

This review details mass spectrometry for analyzing glycopeptides, crucial for understanding how glycosylation impacts protein function in health and disease. It aids in characterizing glycan structures and their attachment sites.

Area of Science:

Biochemistry
Glycobiology
Proteomics

Background:

Glycosylation is a critical post-translational modification influencing protein function.
Understanding glycan structure is key to correlating function in normal and diseased states.
Various methods exist for characterizing protein-bound glycans.

Purpose of the Study:

To review mass spectral analysis of glycopeptides for glycan characterization.
To highlight the utility of this method in studying glycan heterogeneity.
To establish a foundation for understanding glycan function in glycoproteins.

Main Methods:

Glycoprotein proteolysis followed by mass spectral analysis of resulting glycopeptides.
Characterization of glycan heterogeneity.

More Related Videos

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Published on: April 21, 2017

Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics

Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics

Published on: October 13, 2020

Related Experiment Videos

Last Updated: Jun 24, 2026

Glycopeptide Capture for Cell Surface Proteomics

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 10, 2014

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Published on: April 21, 2017

Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics

Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics

Published on: October 13, 2020

Determination of glycan attachment sites on proteins.

Main Results:

Mass spectrometry of glycopeptides effectively characterizes glycan heterogeneity.
This approach links glycan composition to specific protein attachment sites.
Provides insights into glycan structure-function relationships.

Conclusions:

Mass spectral analysis of glycopeptides is a powerful tool for glycan characterization.
This method is foundational for understanding the role of glycosylation in protein function.
Essential for studying both normal and aberrant glycoproteins.