Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Targeting of HSP27 and MMP-2/9 Crosstalk by High-Throughput Drug Repurposing Strategies Identifies Paroxetine as a Potential Candidate in Glioblastoma.

Journal of medicinal chemistry·2026
Same author

A transformer-based method for the cap analysis of gene expression and gene expression tag associated capping region prediction in RNA.

RNA biology·2026
Same author

Foundation models in drug discovery: Phenomenal growth today, transformative potential tomorrow?

Drug discovery today·2025
Same author

Interhemispheric axonal sprouting occurs after pial removal in mice.

Scientific reports·2024
Same author

The molecular prognostic score, a classifier for risk stratification of high-grade serous ovarian cancer.

Journal of ovarian research·2024
Same author

Deciphering the Lexicon of Protein Targets: A Review on Multifaceted Drug Discovery in the Era of Artificial Intelligence.

Molecular pharmaceutics·2024

Related Experiment Video

Updated: May 21, 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

How many protein-protein interactions types exist in nature?

Leonardo Garma1, Srayanta Mukherjee, Pralay Mitra

  • 1Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, United States of America.

Plos One
|June 22, 2012
PubMed
Summary
This summary is machine-generated.

The universe of protein interactions is finite, with an estimated 4,000 possible quaternary folds. Current data covers only 42% of these protein complex structures, requiring extensive future research.

More Related Videos

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

Related Experiment Videos

Last Updated: May 21, 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

Area of Science:

  • Structural Biology
  • Bioinformatics
  • Computational Biology

Background:

  • Protein quaternary structure describes the arrangement of multiple protein subunits in a complex.
  • Understanding the diversity of protein-protein interactions is crucial for deciphering biological functions.

Purpose of the Study:

  • To determine if the number of protein-protein interactions is limited.
  • To estimate the total number of distinct quaternary folds in nature.

Main Methods:

  • All-to-all sequence and structure comparisons of protein complexes from the Protein Data Bank (PDB).
  • Development of a statistical model to relate quaternary families and folds.
  • Estimation of the total number of possible protein-protein interactions.

Main Results:

  • Categorized PDB protein complexes into 3,629 families and 1,761 folds.
  • Estimated the total number of possible protein-protein interactions to be approximately 4,000.
  • Concluded that current repositories contain only 42% of known quaternary folds.

Conclusions:

  • The diversity of protein quaternary structures is finite and estimated at around 4,000 folds.
  • Significant experimental effort is needed to achieve complete coverage of known protein complex structures.
  • Findings impact protein complex modeling and the structural genomics of protein interactions.