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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 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...
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 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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Updated: May 25, 2026

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

Large-scale mapping of human protein interactome using structural complexes.

Manoj Tyagi1, Kosuke Hashimoto, Benjamin A Shoemaker

  • 1National Center for Biotechnology Information, US National Library of Medicine, National Institutes of Health, 8600 Rockville Pike, Bethesda, Maryland 20894, USA.

EMBO Reports
|January 21, 2012
PubMed
Summary
This summary is machine-generated.

Mapping the human protein interactome is improved by a new framework integrating structural data and evolutionary conservation. This approach yields a more coherent network, complementing high-throughput methods for better research leads.

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Last Updated: May 25, 2026

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Systems Biology

Background:

  • High-throughput (HTP) methods for identifying protein interactions generate large datasets but suffer from high false positive rates and incomplete coverage.
  • Existing interactome data requires refinement for accurate functional analysis and hypothesis generation.

Purpose of the Study:

  • To develop a novel framework for mapping the human protein interactome by integrating diverse data types.
  • To improve the accuracy, coverage, and functional coherence of protein interaction networks.

Main Methods:

  • Utilized experimental evidence from structural complexes and atomic details of binding interfaces.
  • Incorporated evolutionary conservation data to infer protein interactions.
  • Developed a framework to construct a structurally inferred interaction network.

Main Results:

  • The structurally inferred interaction network demonstrated higher modularity and functional coherence compared to networks derived solely from literature citations.
  • The inferred network effectively complemented high-confidence HTP networks.
  • A merged network was constructed by combining structural and HTP data.

Conclusions:

  • The novel framework enhances the mapping of the human protein interactome by leveraging structural and evolutionary information.
  • Integrating structural data with HTP methods provides a more reliable and comprehensive interactome map.
  • The merged network offers valuable leads for generating testable hypotheses and guiding future experimental research.