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Related Concept Videos

Protein Networks02:26

Protein Networks

4.4K
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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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Related Experiment Video

Updated: Dec 28, 2025

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

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Detecting Protein-Protein Interaction Based on Protein Fragment Complementation Assay.

Tianwen Wang1, Ningning Yang1, Chen Liang1

  • 1College of Life Sciences, and Institute for Conservation and Utilization of Agro-bioresources in Dabie Mountains, Xinyang Normal University, Xinyang 464000, China.

Current Protein & Peptide Science
|February 14, 2020
PubMed
Summary

Understanding protein interactions is key in cell biology. This study reviews fragment complementation systems like DHFR and GFP for mapping these crucial protein-protein interactions.

Keywords:
Protein-protein interactionenzymefluorescent proteininteraction reporting systemprotein complementation assayubiquitin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proteins are essential molecules that execute genetic instructions.
  • Protein functions are often context-dependent, involving interactions with other proteins within the cell.
  • Identifying protein-protein interactions is vital for understanding individual protein functions and for large-scale proteomics studies.

Purpose of the Study:

  • To introduce and discuss available reporting systems for probing protein-protein interactions.
  • To emphasize the principles and experimental design details for these systems.

Main Methods:

  • Fragment complementation assays using specific protein pairs.
  • Review of systems including dihydrofolate reductase (DHFR), β-lactamase, tobacco etch virus (TEV) protease, luciferase, β-galactosidase, GAL4, horseradish peroxidase (HRP), focal adhesion kinase (FAK), green fluorescent protein (GFP), and ubiquitin.

Main Results:

  • Detailed explanation of various fragment complementation systems for detecting protein interactions.
  • Guidance on experimental design for effective use of these systems.

Conclusions:

  • Fragment complementation systems provide powerful tools for investigating protein-protein interactions.
  • Proper experimental design is crucial for the successful application of these protein interaction mapping techniques.