Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein-protein Interfaces

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 Networks

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,...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

You might also read

Related Articles

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

Sort by

Same author

Exploring glucocorticoid receptor signalling in lymphangioleiomyomatosis.

ERJ open research·2026

Same author

SMARCB1 Deficiency in Tumors Confers a Vulnerability to H3K27 Demethylase Inhibitors via Autophagy Disruption.

Cancer research·2026

Same author

In vitro and in silico study of the endosulfan degradation by Bacillus subtilis sp. strain UAMC.

Biodegradation·2026

Same author

Sources of essential lipids for Mycoplasma pneumoniae via P116 to target liver and atherosclerotic lesions.

Nature communications·2025

Same author

Unprecedented 1,2-mesityl shift for the synthesis of iridafurans.

Dalton transactions (Cambridge, England : 2003)·2025

Same author

Moonlighting Proteins: Some Hypotheses on the Structural Origin of Their Multifunctionality.

International journal of molecular sciences·2025

Same journal

Imbalance in amino acid and purine metabolisms at the hypothalamus in inflammation-associated depression by GC-MS.

Molecular bioSystems·2017

Same journal

Correction: Dynamic properties of dipeptidyl peptidase III from Bacteroides thetaiotaomicron and the structural basis for its substrate specificity - a computational study.

Molecular bioSystems·2017

Same journal

Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats.

Molecular bioSystems·2017

Same journal

Mechanism of the formation of the RecA-ssDNA nucleoprotein filament structure: a coarse-grained approach.

Molecular bioSystems·2017

Same journal

Staphylococcus aureus extracellular vesicles (EVs): surface-binding antagonists of biofilm formation.

Molecular bioSystems·2017

Same journal

Development of an AlphaLISA high throughput technique to screen for small molecule inhibitors targeting protein arginine methyltransferases.

Molecular bioSystems·2017

See all related articles

Search research articles

Related Experiment Video

Updated: May 31, 2026

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

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

Published on: July 6, 2014

Do protein-protein interaction databases identify moonlighting proteins?

Antonio Gómez¹, Sergio Hernández, Isaac Amela

¹Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Barcelona, Spain.

Molecular Biosystems

|June 17, 2011

Summary

This summary is machine-generated.

Discovering "moonlighting" proteins, which perform multiple functions, is crucial for understanding biological complexity. This study reveals that protein-protein interaction databases can help identify these multifunctional proteins and their diverse roles.

More Related Videos

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Published on: January 16, 2017

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

Related Experiment Videos

Last Updated: May 31, 2026

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

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

Published on: July 6, 2014

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Published on: January 16, 2017

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

Area of Science:

Genomics and Proteomics
Molecular Biology
Bioinformatics

Background:

Mammalian genomes have a surprisingly low number of protein-coding genes.
Alternative splicing is a known mechanism for generating protein diversity.
Moonlighting proteins, performing multiple functions, represent another source of functional complexity, often discovered serendipitously.

Purpose of the Study:

To investigate whether protein-protein interaction (PPI) databases can systematically identify moonlighting proteins.
To determine if PPI data can suggest the multiple functions of known moonlighting proteins.
To assess the utility of PPI databases as a tool for discovering protein multifunctionality.

Main Methods:

Analysis of well-established moonlighting proteins within existing protein-protein interaction databases.
Verification of connections between moonlighting proteins and their known interaction partners in PPI databases.
Evaluation of PPI database content for its potential to suggest diverse protein functions.

Main Results:

Established moonlighting proteins are present in PPI databases.
These proteins connect with their known partners within the databases.
The interaction data within PPI databases can indeed suggest the multiple functions of moonlighting proteins.

Conclusions:

Protein-protein interaction databases are a valuable, yet underutilized, resource for identifying moonlighting proteins.
Systematic analysis of PPI databases can aid in the discovery and characterization of protein multifunctionality.
This approach offers a more structured method for uncovering protein roles beyond initial discoveries.