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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...
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...
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: 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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jul 11, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Mapping protein post-translational modifications with mass spectrometry.

Eric S Witze1, William M Old, Katheryn A Resing

  • 1Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA.

Nature Methods
|September 29, 2007
PubMed
Summary

This review explores mass spectrometry techniques for identifying protein post-translational modifications. Understanding these chemical changes is key to unlocking cellular regulation mechanisms.

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

Published on: April 28, 2022

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Last Updated: Jul 11, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
09:40

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

Published on: April 28, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Post-translational modifications (PTMs) are crucial for protein function and cellular regulation.
  • Understanding the diversity and dynamics of PTMs is essential for deciphering complex biological processes.

Purpose of the Study:

  • To provide biologists with an overview of current mass spectrometry-based proteomics strategies.
  • To detail methods for characterizing protein post-translational modifications.
  • To discuss the strengths and limitations of various proteomic approaches for PTM analysis.

Main Methods:

  • Mass spectrometry (MS) is presented as a core technology for PTM detection and quantification.
  • Large-scale proteomic experiments enabling the screening of complex protein mixtures for modifications are highlighted.
  • Strategies for profiling protein chemistry to understand biological control are discussed.

Main Results:

  • Modern MS approaches facilitate comprehensive analysis of PTMs.
  • The review synthesizes current knowledge on mass spectrometry applications in PTM research.
  • Insights into the strengths and weaknesses of different techniques are provided.

Conclusions:

  • Mass spectrometry-based proteomics offers powerful tools for characterizing protein PTMs.
  • This review equips biologists with knowledge to select appropriate MS strategies for PTM studies.
  • Advancements in MS are critical for deeper insights into cell regulation via protein modifications.