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Related Concept Videos

High-Resolution Mass Spectrometry (HRMS)01:15

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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...
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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...
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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.
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Related Experiment Video

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The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
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Properly reading the histone code by MS-based proteomics.

Simone Sidoli1, Benjamin A Garcia1

  • 1Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.

Proteomics
|July 31, 2015
PubMed
Summary
This summary is machine-generated.

Histone post-translational modifications (PTMs) are crucial for DNA packaging and gene regulation. This study validates nanoLC-MS methods for accurate histone PTM analysis, identifying potential pitfalls in sample preparation.

Keywords:
HistonesMass spectrometryPosttranslational modificationsPropionylationSample preparationTechnology

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

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Histone proteins are key to DNA packaging and chromatin structure.
  • Histone post-translational modifications (PTMs) regulate essential cellular processes like gene regulation and DNA repair.
  • Accurate characterization of histone PTMs is vital due to their epigenetic inheritance and role in chromatin biology.

Purpose of the Study:

  • To evaluate and optimize biochemical techniques for characterizing histone PTMs.
  • To assess the reliability of nanoflow LC coupled to MS (nanoLC-MS) for accurate histone PTM quantification.
  • To identify and address challenges in histone sample preparation for nanoLC-MS analysis.

Main Methods:

  • Utilized high-resolution mass spectrometry (MS) for detailed analysis.
  • Employed bioinformatics tools for alignment and characterization of nanoLC-MS runs.
  • Investigated specific adjustments to the histone digestion protocol, including lysine derivatization.

Main Results:

  • Established protocols for effective lysine derivatization in histone analysis.
  • Identified potential side reactions during sample preparation that could be mistaken for biological PTMs.
  • Validated the use of nanoLC-MS for high-confidence identification and high-throughput analysis of histone PTMs.

Conclusions:

  • Optimized nanoLC-MS protocols enhance the accuracy and reliability of histone PTM quantification.
  • Awareness of potential side reactions is crucial for correct interpretation of mass spectrometry data.
  • Advanced MS and bioinformatics approaches are essential for robust histone PTM characterization.