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Related Concept Videos

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...
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...
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...
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...

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Related Experiment Video

Updated: May 8, 2026

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
05:52

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Published on: January 12, 2024

Post-translational modifications and mass spectrometry detection.

André M N Silva1, Rui Vitorino1, M Rosário M Domingues1

  • 1Mass Spectrometry Centre, QOPNA, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.

Free Radical Biology & Medicine
|September 5, 2013
PubMed
Summary
This summary is machine-generated.

Mass spectrometry advancements enhance the detection of post-translational modifications (PTMs). This review covers PTM analysis, including phosphorylation and acetylation, using proteomics and UniProt data.

Keywords:
Literature reviewMass spectrometryPost-translational modifications

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A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis

Published on: April 28, 2022

Area of Science:

  • Biochemistry
  • Proteomics
  • Analytical Chemistry

Background:

  • Post-translational modifications (PTMs) are crucial for protein function.
  • Mass spectrometry (MS) is a key technology for PTM detection.
  • Understanding PTMs requires robust analytical methodologies.

Purpose of the Study:

  • To provide a comprehensive bibliographic overview of MS in PTM detection.
  • To highlight recent technical developments in PTM analysis.
  • To assess the state-of-the-art in MS and proteomics for PTM studies.

Main Methods:

  • Bibliographic analysis of PTM data in UniProt and recent literature (2010-2012).
  • Review of MS principles for PTM detection.
  • Analysis of protein and peptide enrichment strategies for PTMs (phosphorylation, acetylation, oxidation).

Main Results:

  • Significant scientific achievements in PTM detection using MS.
  • Recent technical advancements have improved PTM analysis sensitivity and scope.
  • Evolution of curated PTM data in UniProt indicates growing research interest.

Conclusions:

  • Mass spectrometry is indispensable for PTM identification and characterization.
  • Ongoing technical developments continue to expand the capabilities of PTM analysis.
  • The integration of MS with proteomics databases like UniProt accelerates PTM discovery.