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Related Concept Videos

Protein Networks02:26

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,...
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...
Immunoprecipitation01:20

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: Jun 10, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Proteomic complex detection using sedimentation (ProCoDeS): screening for proteins in stable complexes and their

Marcelo P Segura1, Kathryn S Lilley, Paul Dupree

  • 1Department of Biochemistry, University Of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.

Biochemical Society Transactions
|July 28, 2010
PubMed
Summary

Cellular organization involves protein complexes, not just independent enzymes. ProCoDeS detects endogenous protein complexes using centrifugation and quantitative mass spectrometry, offering a new systems biology tool.

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Last Updated: Jun 10, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

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Published on: November 12, 2012

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09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Area of Science:

  • Proteomics
  • Cellular Biology
  • Systems Biology

Background:

  • Cellular organization involves proteins acting in close association.
  • Co-precipitation and tandem affinity purification (TAP) are standard methods for identifying protein complexes.
  • TAP tagging has limitations for high-throughput systems biology, especially in non-transformable organisms.

Purpose of the Study:

  • To introduce and review ProCoDeS (Proteomic Complex Detection using Sedimentation) as a novel technique.
  • To highlight the advantages of ProCoDeS for studying endogenous protein complexes.
  • To discuss the prospects of ProCoDeS and similar quantitative mass spectrometry techniques.

Main Methods:

  • ProCoDeS separates protein samples via centrifugation.
  • Fractions from the gradient are analyzed using quantitative mass spectrometry (MS).
  • Protein partners are identified by statistical analysis of co-fractionation, avoiding complex purification.

Main Results:

  • ProCoDeS detects endogenous protein complexes without genetic manipulation.
  • The method relies on co-fractionation patterns for partner identification.
  • Quantitative MS enables large-scale analysis of protein complex composition.

Conclusions:

  • ProCoDeS offers a valuable approach for studying protein complexes in various biological systems.
  • Quantitative MS-based techniques are promising for measuring protein complex composition.
  • ProCoDeS overcomes limitations of TAP tagging in systems biology research.