Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
MALDI-TOF Mass Spectrometry01:19

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 Spectrometry01:33

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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Mass Spectrometry: Complex Analysis01:21

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

Phospho-mimic βIII-tubulin rescues microtubule and cardiac defects in Duchenne muscular dystrophy mice.

Journal of molecular and cellular cardiology·2026
Same author

Therapeutic targeting of the eIF4E cap-binding domain reveals control of lineage fate in prostate cancer.

The Journal of clinical investigation·2026
Same author

Machine learning-based multimodal biomarkers enable accurate diagnosis and early detection of pancreatic ductal adenocarcinoma.

Scientific reports·2026
Same author

Artemis: Mass Spectrometry-Based Identification of MHC-Presented Peptides Across Alleles, Classes, and Species Using Soluble Single-Chain MHC Constructs.

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

Injury-induced connexin 43 expression regulates endothelial wound healing.

American journal of physiology. Heart and circulatory physiology·2025
Same author

The serine protease HtrA regulates Group B Streptococcus virulence and affects the host response to infection.

PLoS pathogens·2025

Related Experiment Video

Updated: Jun 18, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 13, 2009

Methodologies for characterizing phosphoproteins by mass spectrometry.

Philip R Gafken1, Paul D Lampe

  • 1Proteomics Facility, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.

Cell Communication & Adhesion
|December 13, 2006
PubMed
Summary

Protein phosphorylation regulates protein function rapidly and reversibly. Mass spectrometry (MS) is key for identifying phosphorylation sites, linking these events to functional changes in phosphoproteins.

More Related Videos

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
12:23

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Related Experiment Videos

Last Updated: Jun 18, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 13, 2009

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
12:23

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Posttranslational modification, specifically protein phosphorylation, is a fundamental mechanism controlling protein function.
  • Phosphorylation offers a rapid and reversible switch for modulating protein activity.
  • Understanding phosphorylation events requires precise detection of phosphorylated proteins and identification of specific phosphorylation sites.

Purpose of the Study:

  • To review current and emerging methodologies for phosphoprotein analysis.
  • To highlight techniques for identifying phosphorylation sites and linking them to functional changes.
  • To provide an overview of mass spectrometry (MS)-based approaches in phosphoproteomics.

Main Methods:

  • Review of sample separation and enrichment techniques: SDS-PAGE, immunoprecipitation, metal-assisted enrichment, strong cation exchange, and dendrimer capture.
  • Overview of quantitative MS analysis methods: SILAC, iTRAQ, and AQUA.
  • Discussion of advanced techniques: electron transfer dissociation ionization and "top-down" proteomics for phosphoprotein analysis.

Main Results:

  • Mass spectrometry (MS) has emerged as the preferred technology for phosphosite identification.
  • A range of sample preparation and enrichment strategies are available to enhance phosphoprotein detection.
  • Quantitative MS methods enable the measurement of changes in phosphorylation levels.

Conclusions:

  • Accurate identification of phosphorylation sites is crucial for elucidating the functional consequences of protein phosphorylation.
  • The integration of diverse MS-based techniques, from sample preparation to advanced ionization methods, is advancing phosphoproteomics.
  • Continued development in proteomics methodologies will further enhance our understanding of dynamic protein regulation.