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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,...
Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Capillary Electrophoresis: Applications01:30

Capillary Electrophoresis: Applications

Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...
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...
Western Blotting01:15

Western Blotting

Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.

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Related Experiment Video

Updated: Jun 19, 2026

Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

Native electrophoretic techniques to identify protein-protein interactions.

Ilka Wittig1, Hermann Schägger

  • 1Cluster of Excellence Macromolecular Complexes, Zentrum der Biologischen Chemie, Molekulare Bioenergetik, Goethe-Universität Frankfurt, Frankfurt am Main, Germany.

Proteomics
|October 17, 2009
PubMed
Summary
This summary is machine-generated.

Native electrophoresis techniques like blue-native and clear-native electrophoresis identify stable protein complexes. These methods are crucial for studying membrane proteins and supercomplexes, but not dynamic interactions without cross-linking.

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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

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

Published on: April 1, 2017

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation
14:44

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Related Experiment Videos

Last Updated: Jun 19, 2026

Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

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

Published on: April 1, 2017

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation
14:44

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Protein-protein interactions are fundamental to cellular processes.
  • Identifying stable protein complexes is essential for understanding protein function.
  • Existing methods like co-immunoprecipitation and tandem affinity purification are widely used.

Purpose of the Study:

  • To detail the application of native electrophoresis techniques for identifying protein complexes.
  • To highlight the utility of blue-native and clear-native electrophoresis for studying membrane proteins and supercomplexes.
  • To differentiate the capabilities of native electrophoresis from other techniques for dynamic interactions.

Main Methods:

  • Focus on blue-native electrophoresis (BNE)
  • Focus on clear-native electrophoresis (CNE)
  • Focus on high-resolution clear-native electrophoresis (HR-CNE) and associated techniques

Main Results:

  • BNE, CNE, and HR-CNE effectively identify stable protein complexes.
  • These native electrophoresis methods can resolve detergent-labile physiological supercomplexes.
  • Native electrophoresis techniques are not suitable for detecting dynamic protein-protein interactions unless in vivo cross-linking is performed.

Conclusions:

  • Native electrophoresis techniques are powerful tools for characterizing stable protein complexes, including membrane protein assemblies.
  • These methods offer advantages in preserving the native state of protein complexes during analysis.
  • Understanding the limitations of native electrophoresis is key to selecting appropriate methods for studying protein interactions.