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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...

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Related Experiment Video

Updated: May 14, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Protein lysine acetylation analysis: current MS-based proteomic technologies.

Kai Zhang1, Shanshan Tian, Enguo Fan

  • 1State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China. Zhangkai730@yahoo.com.cn

The Analyst
|January 31, 2013
PubMed
Summary
This summary is machine-generated.

Protein lysine acetylation (Kac) is crucial for cellular regulation and holds therapeutic potential for diseases like cancer. Identifying Kac globally is challenging, but mass spectrometry-based proteomics offers advanced solutions.

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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Protein lysine acetylation (Kac) is a vital post-translational modification regulating gene expression, cell cycle, and metabolism.
  • Dysregulated acetylation is implicated in diseases, notably cancer, highlighting its therapeutic relevance.
  • Global identification of Kac sites remains challenging due to low abundance and dynamic nature.

Purpose of the Study:

  • To review current strategies for identifying protein lysine acetylation.
  • To cover techniques from histone to system-wide Kac analysis.
  • To discuss advancements in mass spectrometry-based proteomics for Kac detection.

Main Methods:

  • Review of enrichment techniques for acetylated peptides.
  • Analysis of chromatographic separation strategies for complex proteomes.
  • Overview of mass spectrometry (MS) methods for Kac identification.

Main Results:

  • Various MS-based proteomic technologies have been developed for Kac identification.
  • Effective enrichment and separation strategies are crucial for detecting low-abundance Kac sites.
  • Current methods enable both targeted histone acetylation and broad system-wide Kac profiling.

Conclusions:

  • Mass spectrometry-based proteomics is essential for global Kac identification.
  • Advancements in enrichment and separation techniques improve Kac detection sensitivity.
  • Understanding protein acetylation is key for developing targeted disease therapies.