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Related Concept Videos

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Covalently Linked Protein Regulators

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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.
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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.
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Updated: Apr 20, 2026

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Method to study stoichiometry of protein post-translational modification.

Hao Li1, Yue Huang, Bin Zhang

  • 1State Key Laboratory of Pharmaceutical Biotechnology and Department of Biochemistry, Nanjing University , No. 22 Hankou Rd., Nanjing, Jiangsu 210093, China.

Analytical Chemistry
|November 18, 2014
PubMed
Summary

We developed a novel method using small-molecule labels to determine protein post-translational modification (PTM) stoichiometry. This technique quantifies PTMs by comparing signal ratios, revealing integer stoichiometry for key regulatory proteins.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Post-translational modifications (PTMs) regulate protein function.
  • Accurate quantification of PTM stoichiometry is crucial for understanding cellular processes.
  • Existing methods for PTM stoichiometry analysis have limitations.

Purpose of the Study:

  • To develop a novel method for determining the stoichiometry of protein post-translational modifications (PTMs).
  • To validate the method's efficacy in analyzing site-specific PTMs on regulatory proteins.

Main Methods:

  • Utilizing small-molecule labels that bind to modified amino acids.
  • Employing a differential labeling strategy based on label-macromolecule interactions.
  • Determining stoichiometry via the ratio of signals obtained from two distinct labeling conditions.

Main Results:

  • The method successfully determined integer stoichiometric numbers for PTMs.
  • Site-specific nitration was confirmed on several essential regulatory proteins.
  • The approach provides detailed and biologically significant information on PTMs.

Conclusions:

  • The developed method offers a robust approach for PTM stoichiometry analysis.
  • Integer stoichiometry indicates regulated, site-specific PTMs in key cellular proteins.
  • This technique enhances our understanding of PTMs' biological roles.