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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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Updated: May 27, 2026

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Split-protein systems: beyond binary protein-protein interactions.

Sujan S Shekhawat1, Indraneel Ghosh

  • 1Department of Chemistry and Biochemistry, University of Arizona, 1306 East University Blvd, Tucson, AZ 85721, USA.

Current Opinion in Chemical Biology
|November 11, 2011
PubMed
Summary
This summary is machine-generated.

Split-protein reassembly, a protein fragment complementation method, offers sensitive detection of biomacromolecular interactions. Recent advances enable rapid identification of complexes, inhibitors, and nucleic acids, with therapeutic potential.

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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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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

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Last Updated: May 27, 2026

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

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

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Biotechnology

Background:

  • The human interactome comprises millions of protein-protein interactions crucial for cellular functions.
  • Accurate methods are needed to study these interactions, modifications, and locations in complex biological systems.
  • Understanding interactome differences in disease states and therapeutic responses is vital.

Purpose of the Study:

  • To present recent advancements in engineering split-protein systems for biomacromolecular interaction detection.
  • To highlight the utility of these systems in identifying protein complexes, small molecule inhibitors, and nucleic acids.
  • To explore the integration of split-protein systems with chemical inducers of dimerization for enhanced control and inhibitor screening.

Main Methods:

  • Utilized split-protein reassembly (protein fragment complementation) with reporter proteins like GFP and luciferase.
  • Engineered split-protein systems for detecting ternary protein complexes and various macromolecules.
  • Combined split-protein systems with chemical inducers of dimerization to regulate orthogonal split-proteases and identify enzyme inhibitors.

Main Results:

  • Demonstrated rapid detection of ternary protein complexes, small molecule inhibitors, nucleic acids, and other macromolecules.
  • Showcased the ability to regulate split-protease activity and identify enzyme inhibitors using combined strategies.
  • Discussed autoinhibition strategies for developing 'turn-on' sensors.

Conclusions:

  • Split-protein reassembly is a versatile and sensitive method for studying biomacromolecular interactions across various systems.
  • Recent engineering advances expand its applications to complex molecular detection and therapeutic strategies.
  • Future directions include developing novel split-protein methodologies with potential therapeutic applications.