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Related Concept Videos

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...
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...
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For example, the mass of helium...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Mass Spectrometry: Molecular Fragmentation Overview01:20

Mass Spectrometry: Molecular Fragmentation Overview

The ionization of a molecule into a molecular ion inside the mass spectrometer causes instability in the molecule's structure due to the loss of an electron. This eventually leads to the fragmentation or breaking of some bonds in the molecule. The fragmentation occurs predominantly at specific bonds to yield relatively stable fragments.
One type of fragmentation pattern is the cleavage of a single bond in the molecular ion. The cleavage leads to a radical and a cation. The cleavage can occur at...

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Related Experiment Video

Updated: May 28, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Breaking the histone code with quantitative mass spectrometry.

Laura-Mae P Britton1, Michelle Gonzales-Cope, Barry M Zee

  • 1Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.

Expert Review of Proteomics
|October 18, 2011
PubMed
Summary
This summary is machine-generated.

Mass spectrometry is revolutionizing the study of histone post-translational modifications (PTMs), offering deeper insights than traditional antibody methods. This approach overcomes technical limitations, paving the way for advanced chromatin biology research.

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The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
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The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin

Published on: April 11, 2014

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

Related Experiment Videos

Last Updated: May 28, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
24:02

The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin

Published on: April 11, 2014

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

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Proteomics

Background:

  • Histone post-translational modifications (PTMs) are crucial epigenetic regulators of gene expression.
  • Traditional methods like site-specific antibodies face challenges such as cross-reactivity and epitope occlusion.
  • Mass spectrometry-based proteomics offers a powerful alternative for studying histone PTMs.

Purpose of the Study:

  • To review the advancements of mass spectrometry in analyzing histone PTMs.
  • To highlight the advantages of mass spectrometry over conventional techniques.
  • To identify future challenges for mass spectrometry in chromatin biology.

Main Methods:

  • Review of existing literature on mass spectrometry applications in histone PTM analysis.
  • Comparison of mass spectrometry with antibody-based approaches.
  • Discussion of technical hurdles and future directions.

Main Results:

  • Mass spectrometry has revealed novel aspects of histone PTMs previously inaccessible.
  • This technique provides a more comprehensive and accurate interrogation of histone modifications.
  • Significant progress has been made in understanding the complex histone PTM landscape.

Conclusions:

  • Mass spectrometry is becoming indispensable for histone PTM research.
  • Overcoming current limitations will establish mass spectrometry as the preferred method in chromatin biology.
  • This technology promises to deepen our understanding of epigenetic regulation.