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Updated: Mar 29, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
Published on: November 15, 2017
The quantitative and condition-dependent Escherichia coli proteome.
Alexander Schmidt1, Karl Kochanowski2, Silke Vedelaar3
1Biozentrum, University of Basel, Basel, Switzerland.
Researchers mapped protein concentrations in Escherichia coli across 22 conditions, revealing new insights into bacterial biology and post-translational modifications. This study provides a valuable resource for systems biology and E. coli research.
Area of Science:
- Proteomics
- Systems Biology
- Bacterial Physiology
Background:
- Precise protein concentration measurements are crucial for understanding biological processes.
- Escherichia coli is a model organism extensively studied in molecular biology and genetics.
Purpose of the Study:
- To create a comprehensive, condition-dependent protein-abundance map for Escherichia coli.
- To identify previously unknown prevalent post-translational modifications in bacteria.
Main Methods:
- Utilized efficient protein extraction and sample fractionation.
- Employed state-of-the-art quantitative mass spectrometry techniques.
Main Results:
- Measured cellular protein concentrations for over 2,300 E. coli genes (55% of predicted genes) across 22 experimental conditions.
- Identified widespread methylation and N-terminal protein acetylations in bacteria.
- Uncovered system-wide proteome allocation, expression regulation, and post-translational adaptations.
Conclusions:
- The generated protein-abundance map is a valuable resource for the systems biology and E. coli research communities.
- The findings offer new insights into bacterial proteome dynamics and regulation.
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