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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

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Nitropeptide Profiling and Identification Illustrated by Angiotensin II
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Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Site-specific proteomics approach for study protein S-nitrosylation.

Miao Liu1, Jinxuan Hou, Lin Huang

  • 1Department of Pathology and Microbiology, Mass Spectrometry and Proteomics Core Facility, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA.

Analytical Chemistry
|August 7, 2010
PubMed
Summary

This study introduces a new method to identify protein S-nitrosylation sites in complex mixtures. The approach successfully identified 162 sites, advancing the study of nitric oxide

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Last Updated: Jun 10, 2026

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Protein S-nitrosylation is a crucial post-translational modification involved in various cellular processes.
  • Accurate identification of S-nitrosylation sites is essential for understanding its biological functions.
  • Existing methods have limitations in identifying S-nitrosylation sites in complex biological samples.

Purpose of the Study:

  • To develop and validate a novel, robust method for identifying protein S-nitrosylation sites.
  • To apply the method to identify S-nitrosylation sites in breast cancer cells treated with a nitric oxide donor.
  • To reveal a potential S-nitrosylation motif and facilitate further functional studies.

Main Methods:

  • Utilized cysteinyl affinity resin for selective enrichment of S-nitrosylated peptides.
  • Employed ascorbate reduction followed by nanoscale liquid chromatography-tandem mass spectrometry (LC-MS/MS).
  • Used two alkylation agents with distinct mass tags to distinguish S-nitrosylated from non-S-nitrosylated peptides.

Main Results:

  • Successfully identified 162 S-nitrosylation sites in MDA-MB-231 cells treated with Angeli's salt.
  • Revealed a novel S-nitrosylation motif.
  • The number of identified sites significantly surpasses previous reports, demonstrating high efficiency.

Conclusions:

  • The developed method is highly efficient for identifying protein S-nitrosylation sites in complex mixtures.
  • This advancement will aid in the functional characterization of protein S-nitrosylation.
  • The findings may lead to the discovery of new therapeutic targets for diseases involving S-nitrosylation.