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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,...
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...
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 4, 2026

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

A coprecipitation-based validation methodology for interactions identified using protein microarrays.

Ovidiu Marina1, Jonathan S Duke-Cohan, Catherine J Wu

  • 1Department of Radiation Oncology, William Beaumont Hospital, Royal Oak, MI, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 4, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a faster method to confirm protein interactions found using protein microarrays. The new protocol uses in vitro synthesized proteins to efficiently validate potential interactions and reduce false positives.

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

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Related Experiment Videos

Last Updated: Jun 4, 2026

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

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
  • Immunology

Background:

  • High-throughput protein microarrays identify numerous candidate protein interactions.
  • Conventional validation methods are often time-consuming and labor-intensive.
  • Efficient confirmation is crucial for reliable downstream analysis.

Purpose of the Study:

  • To develop a medium-throughput protocol for validating protein interactions identified by protein microarrays.
  • To enable rapid elimination of false positives from screening data.
  • To provide a sensitive confirmatory test for protein-protein interactions.

Main Methods:

  • Utilized a rabbit reticulocyte lysate-coupled transcription and translation system for in vitro synthesis of biotin-labeled proteins.
  • Employed a coprecipitation assay to validate protein interactions.
  • Developed methods for immunoglobulin purification from serum.
  • Quantified immunoprecipitated target protein using Western blot analysis.

Main Results:

  • Established a sensitive medium-throughput validation protocol for protein interactions.
  • Demonstrated the ability to rapidly eliminate false positive interactions.
  • Successfully purified immunoglobulin and quantified coprecipitated proteins.

Conclusions:

  • The described technique offers a sensitive and rapid confirmatory test for protein interactions.
  • This method facilitates the efficient elimination of false positives prior to extensive validation.
  • The protocol supports the analysis of target interactions in their native environment.