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...

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...

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...

You might also read

Related Articles

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

Sort by

Same author

Update and New Implementation of the MIRAGE Reporting Guidelines for Mass Spectrometry Experiments in Glycoscience.

Molecular & cellular proteomics : MCP·2025

Same author

Microbial Lectin-Targeting Mucus: A Glycobioinformatic Approach.

Methods in molecular biology (Clifton, N.J.)·2025

Same author

Tools for structural lectinomics: From structures to lectomes.

BBA advances·2025

Same author

Meeting report of the GlySpace Alliance and GaLSIC symposium.

Glycobiology·2025

Same author

MatrixDB 2024: an increased coverage of extracellular matrix interactions, a new Network Explorer and a new web interface.

Nucleic acids research·2024

Same author

Functional implications of glycans and their curation: insights from the workshop held at the 16th Annual International Biocuration Conference in Padua, Italy.

Database : the journal of biological databases and curation·2024

Same journal

Mapping the 3D Chromosome Organization of a Biosynthetic Gene Cluster by Capture Hi-C (CHi-C).

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Mapping the 3D Chromosome Organization of Streptomyces by Hi-C.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

CUT&Tag Epigenomic Profiling of Biosynthetic Gene Clusters in Arabidopsis thaliana.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Rhizobium rhizogenes-Mediated Hairy Root Transformation Protocol for Lotus japonicus and Other Legumes.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Characterization of Bioactive Saponins from Sea Cucumbers.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Methods for Functional Validation of Terpenoid Metabolic Clusters in Nicotiana benthamiana and Aspergillus oryzae.

Methods in molecular biology (Clifton, N.J.)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 6, 2026

Quantitative Analysis of Chromatin Proteomes in Disease

Quantitative Analysis of Chromatin Proteomes in Disease

Published on: December 28, 2012

LC/MS data processing for label-free quantitative analysis.

Patricia M Palagi¹, Markus Müller, Daniel Walther

¹Proteome Informatics Group, Swiss Institute of Bioinformatics, Geneva, Switzerland.

Methods in Molecular Biology (Clifton, N.J.)

|November 11, 2010

Summary

This summary is machine-generated.

SuperHirn and MSight are complementary tools for label-free proteomics quantitation. They aid in processing liquid chromatography-mass spectrometry (LC/MS) data for accurate protein abundance measurements.

More Related Videos

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Metabolic Labeling and Membrane Fractionation for Comparative Proteomic Analysis of Arabidopsis thaliana Suspension Cell Cultures

Metabolic Labeling and Membrane Fractionation for Comparative Proteomic Analysis of Arabidopsis thaliana Suspension Cell Cultures

Published on: September 28, 2013

Related Experiment Videos

Last Updated: Jun 6, 2026

Quantitative Analysis of Chromatin Proteomes in Disease

Quantitative Analysis of Chromatin Proteomes in Disease

Published on: December 28, 2012

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Metabolic Labeling and Membrane Fractionation for Comparative Proteomic Analysis of Arabidopsis thaliana Suspension Cell Cultures

Metabolic Labeling and Membrane Fractionation for Comparative Proteomic Analysis of Arabidopsis thaliana Suspension Cell Cultures

Published on: September 28, 2013

Area of Science:

Proteomics
Analytical Chemistry
Bioinformatics

Background:

Label-free liquid chromatography-mass spectrometry (LC/MS) is crucial for proteomics.
Accurate quantitation requires robust data processing tools.
Existing tools may have limitations in specific aspects of LC/MS data analysis.

Purpose of the Study:

To describe the complementary use of SuperHirn and MSight for label-free LC/MS data processing.
To demonstrate a workflow for enhanced proteomics quantitation using these tools.
To highlight the capabilities of SuperHirn in peak detection, normalization, and alignment, and MSight in data visualization and navigation.

Main Methods:

Utilizing SuperHirn for peak detection, normalization, and alignment of LC/MS runs.
Employing MSight for visualization and navigation of the processed LC/MS data.
Integrating SuperHirn and MSight in a complementary workflow for proteomics quantitation.

Main Results:

Demonstrated successful application of SuperHirn and MSight for label-free LC/MS data processing.
Showcased the synergistic benefits of combining visualization (MSight) with advanced processing (SuperHirn).
Provided a practical example of using these tools for quantitative proteomics.

Conclusions:

SuperHirn and MSight offer a powerful, complementary solution for label-free proteomics quantitation.
The integrated approach facilitates more accurate and efficient analysis of complex LC/MS data.
These tools enhance the capabilities for researchers in quantitative proteomics studies.