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Related Concept Videos

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...
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,...

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Related Experiment Video

Updated: Jun 5, 2026

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

Extracting gene function from protein-protein interactions using Quantitative BAC InteraCtomics (QUBIC).

Nina C Hubner1, Matthias Mann

  • 1Department of Proteomics and Signal Transduction, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.

Methods (San Diego, Calif.)
|December 28, 2010
PubMed
Summary
This summary is machine-generated.

Quantitative BAC InteraCtomics (QUBIC) offers a streamlined method for identifying protein interactions under physiological conditions. This approach utilizes tagged proteins and mass spectrometry for high-confidence interactome mapping.

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Last Updated: Jun 5, 2026

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
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Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Area of Science:

  • Proteomics
  • Systems Biology
  • Molecular Biology

Background:

  • Large-scale proteomic screens are crucial for gene pathway elucidation.
  • Protein-protein interactions are frequently studied using affinity purification followed by mass spectrometry (AP-MS).
  • Existing AP-MS methods require improvement for physiological context and ease of use.

Purpose of the Study:

  • To present detailed workflows for the Quantitative BAC InteraCtomics (QUBIC) approach.
  • To enable high-confidence identification of protein binding partners under physiological conditions.
  • To facilitate small and large-scale protein interactome mapping.

Main Methods:

  • Utilizing tagged, full-length proteins expressed under endogenous control via BAC transgenes or gene trap loci.
  • Implementing fast, streamlined, and generic purification procedures.
  • Employing single-run liquid chromatography-mass spectrometry (LC-MS) with either SILAC (stable isotope labeling of amino acids in cell culture) or label-free quantification.
  • Analyzing data using the MaxQuant environment.

Main Results:

  • Demonstration of a robust workflow for obtaining specific protein binding partners.
  • Successful application of QUBIC for high-confidence interactome mapping.
  • Availability of detailed protocols and cell line collections for researchers.

Conclusions:

  • QUBIC provides a powerful and accessible method for protein interactome mapping.
  • The approach enhances the physiological relevance of protein-protein interaction studies.
  • Biologists with access to high-resolution mass spectrometry can readily implement QUBIC.