Related Experiment Video

Updated: Jan 21, 2026

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
05:52

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF

Published on: January 12, 2024

1.6K

Identification of Posttranslational Modifications (PTMs) of Proteins by Mass Spectrometry

Roshanak Aslebagh1, Kelly L Wormwood2, Devika Channaveerappa2

  • 1Biochemistry & Proteomics Group, Department of Chemistry & Biomolecular Science, Clarkson University, Potsdam, NY, USA. aslebar@clarkson.edu.

Advances in Experimental Medicine and Biology
|July 27, 2019
PubMed

Insights

The human proteome complexity arises from alternative splicing and posttranslational modifications (PTMs), vastly exceeding gene count. Mass spectrometry and proteomics identify diverse PTMs, revealing intricate protein variations.

Area of Science:

  • Proteomics
  • Molecular Biology
  • Biochemistry

Background:

  • The central dogma suggests a 1:1 gene:protein ratio, but human cells express millions of protein entities.
  • This discrepancy is largely explained by alternative splicing and posttranslational modifications (PTMs).

Purpose of the Study:

  • To discuss the complexity of protein isoforms generated by alternative splicing and PTMs.
  • To highlight the role of mass spectrometry and proteomics in identifying PTMs.

Main Methods:

  • Mass spectrometry-based proteomics.
  • Analysis of various posttranslational modifications including acetylation, phosphorylation, glycosylation, alkylation, hydroxinonenal-modification, and disulfide bridges.

Main Results:

  • Demonstration of how alternative splicing generates diverse protein isoforms.
  • Identification of multiple PTMs and their impact on protein function and structure.
  • Specific examples of identified PTMs using mass spectrometry.

Conclusions:

  • Alternative splicing and PTMs significantly expand proteome diversity beyond gene number.
  • Mass spectrometry and proteomics are crucial for characterizing complex protein modifications and isoforms.
Keywords:
Mass spectrometryPosttranslational modificationsProteomics

More Related Videos

Identification of Post-translational Modifications of Plant Protein Complexes10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.5K
Characterizing RNA Modifications in Single Neurons Using Mass Spectrometry08:45

Characterizing RNA Modifications in Single Neurons Using Mass Spectrometry

Published on: April 21, 2022

2.8K

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...
8.1K
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
2.4K
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...
8.4K
Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
5.3K
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
3.9K
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.9K