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Proteomics

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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Ribosome Profiling

Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique helps...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: May 15, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Contemporary positional proteomics strategies to study protein processing.

Kim Plasman¹, Petra Van Damme, Kris Gevaert

¹Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium.

Current Opinion in Chemical Biology

|January 8, 2013

Summary

This summary is machine-generated.

Positional proteomics, a mass spectrometry technique, identifies protein termini. This method is ideal for studying proteases and their effects on biological processes by analyzing protein degradation products.

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Area of Science:

Proteomics
Biochemistry
Mass Spectrometry

Background:

Proteases are enzymes that cleave peptide bonds, significantly impacting biological pathways.
Understanding protease activity is crucial for studying various biological processes and diseases.
Traditional methods may not fully capture the dynamic nature of protease-substrate interactions.

Purpose of the Study:

To review recent advancements in positional proteomics.
To highlight the application of positional proteomics in protease degradomics.
To discuss the utility of mass spectrometry-driven techniques for analyzing protease functions.

Main Methods:

Positional proteomics enriches peptides from protein termini.
Mass spectrometry (MS) is used for the identification of these peptides.
The review focuses on recent developments in these MS-driven technologies.

Main Results:

Positional proteomics enables the identification of novel protein termini generated by proteases.
This technique is highly effective for protease degradomics, revealing substrate cleavage sites.
Recent developments have enhanced the sensitivity and scope of positional proteomics.

Conclusions:

Positional proteomics is a powerful tool for studying protease activity and substrate degradation.
The integration of positional proteomics with mass spectrometry offers deep insights into protease-mediated biological events.
Continued advancements in this field promise to further elucidate protease functions in health and disease.