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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-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,...
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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jul 14, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

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

Published on: March 3, 2015

Protein-protein interactions: better by the dozen.

Veronique Kiermer

    Nature Methods
    |May 22, 2007
    PubMed
    Summary

    This study combined two large yeast protein-protein interaction datasets. The consolidated data offers high accuracy, comparable to smaller, more reliable experiments.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Yeast Genetics

    Background:

    • Protein-protein interactions (PPIs) are crucial for cellular functions.
    • Large-scale studies are essential for comprehensive PPI mapping.
    • Previous large-scale yeast PPI studies had limitations in data consolidation and accuracy.

    Purpose of the Study:

    • To create a consolidated, high-accuracy dataset of yeast protein-protein interactions.
    • To improve the reliability of large-scale PPI data through reanalysis.
    • To provide a robust resource for yeast systems biology research.

    Main Methods:

    • Combined reanalysis of two major yeast protein-protein interaction datasets.
    • Data integration and quality control protocols were applied.

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    Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

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

    Published on: July 6, 2014

    Related Experiment Videos

    Last Updated: Jul 14, 2026

    Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
    08:38

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

    Published on: March 3, 2015

    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

    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

  • Validation against established benchmarks for PPI reliability.
  • Main Results:

    • A large, consolidated dataset of yeast PPIs was generated.
    • The reanalyzed data demonstrated accuracy comparable to small-scale experimental validations.
    • Enhanced confidence in the identified PPIs was achieved.

    Conclusions:

    • The consolidated yeast PPI dataset represents a significant advancement in the field.
    • This resource will facilitate deeper understanding of yeast cellular mechanisms.
    • The findings support the utility of combined reanalysis for improving large-scale biological data.