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...

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,...

You might also read

Related Articles

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

Sort by

Same author

Atmospheric Aging Alters the Toxicity Mechanisms of Residential Wood Combustion Aerosol: A Parallel <i>In Vivo</i> and <i>In Vitro</i> Study.

Environmental science & technology·2026

Same author

Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed.

Clinical and translational allergy·2026

Same author

Assessing the Allergenic Relevance of Vespula alascensis Venom: Implications for Venom Immunotherapy.

Journal of investigational allergology & clinical immunology·2025

Same author

Development of a highly differentiated rat brain organoid model for exploring glioblastoma invasion dynamics and therapy.

Neuro-oncology·2025

Same author

The Novel MuRF2 Target SNX5 Regulates PKA Activity Through Stabilization of RI-α and Controls Myogenic Differentiation.

Journal of cachexia, sarcopenia and muscle·2025

Same author

A strategy for multimodal integration of transcriptomics, proteomics, and radiomics data for the prediction of recurrence in patients with IDH-mutant gliomas.

International journal of cancer·2025

Same journal

Tracking Synthetic Adhesins on Bacterial Surfaces with Immunofluorescence Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Post-Selection Methods for Analyzing mRNA Display Selections and Optimization of Hits.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

High-Performance Computing in Tandem Mass Spectrometry (MS/MS) Peptide Identification.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

AI-Driven Protein Research: From Prediction to Design.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Methods for the In Vitro Selection of Protein and Peptide Libraries Using mRNA Display.

Methods in molecular biology (Clifton, N.J.)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jul 23, 2025

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Protein Interaction Screen on a Peptide Matrix (PrISMa).

Daniel Perez-Hernandez¹, Mattson Jones¹, Gunnar Dittmar^2,3

¹Department of Infection and Immunity, Luxembourg Institute of Health, Strassen, Luxembourg.

Methods in Molecular Biology (Clifton, N.J.)

|July 14, 2023

Summary

This summary is machine-generated.

This study introduces PrISMa, a novel high-throughput method for detecting weak and transient protein-protein interactions (PPI). PrISMa enhances understanding of the interactome, particularly within intrinsically disordered regions.

Keywords:

Interactomics Mass-spectrometry Peptide-array Proteomics

More Related Videos

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

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

Published on: March 3, 2015

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Related Experiment Videos

Last Updated: Jul 23, 2025

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

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

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

Published on: March 3, 2015

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Protein-protein interactions (PPI) are fundamental to cellular functions.
High-throughput methods have advanced interactome and proteome studies, but often miss weak/transient interactions.
Intrinsically disordered regions (IDRs) constitute a significant portion of the proteome but are challenging to study for interactions.

Purpose of the Study:

To present a novel protocol, PrISMa (Protein Interaction Screen on a peptide Matrix), for high-throughput PPI screening.
To address limitations of existing methods in detecting weak, transient interactions.
To map interactions within linear protein sequences, including those in IDRs.

Main Methods:

Development and application of the PrISMa protocol.
Utilizing a peptide matrix for high-throughput screening of protein interactions.
Focusing on identifying interactions missed by conventional PPI methods.

Main Results:

PrISMa successfully functions as a high-throughput screen.
The method is unique in targeting weak and transient protein-protein interactions.
PrISMa excels at mapping interactions across linear protein sequences, including IDRs.

Conclusions:

PrISMa expands the understanding of the proteome by identifying transient interactors.
The protocol offers a valuable tool for studying complex protein interactions, especially within IDRs.
This method contributes to a more comprehensive understanding of cellular mechanisms through PPI analysis.