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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-Protein Interfaces

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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,...

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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...

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Related Experiment Video

Updated: May 6, 2026

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

Navigating the global protein-protein interaction landscape using iRefWeb.

Andrei L Turinsky¹, Sabry Razick, Brian Turner

¹Molecular Structure and Function program, Hospital for Sick Children, Toronto, ON, Canada.

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

|November 9, 2013

Summary

This summary is machine-generated.

iRefWeb consolidates protein-protein interaction data from 14 databases across 1000+ organisms. This bioinformatics resource provides advanced filters for reliable interaction analysis and data retrieval.

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Area of Science:

Bioinformatics
Computational Biology
Systems Biology

Background:

Protein-protein interactions (PPIs) are fundamental to cellular processes.
Curating and accessing PPI data from diverse sources is challenging.
Existing resources often lack comprehensive integration and advanced search functionalities.

Purpose of the Study:

To present iRefWeb, a consolidated bioinformatics resource for protein-protein interaction data.
To provide versatile tools for searching, filtering, and assessing the reliability of PPIs.
To facilitate access to PPI data across a wide range of organisms.

Main Methods:

Data consolidation from 14 major public PPI databases.
Development of advanced search and filtering options for PPIs and protein complexes.
Integration of evidence-based reliability criteria for PPI assessment.
Inclusion of publication-specific annotations and data.

Main Results:

iRefWeb provides access to a large, integrated collection of PPI data.
The resource supports retrieval of interactions by organism or protein.
Users can filter interactions based on evidence and assess reliability.
Detailed annotations for publications describing interaction experiments are available.

Conclusions:

iRefWeb serves as a valuable, freely accessible bioinformatics resource for researchers.
The platform enhances the study of protein-protein interactions and complexes.
It simplifies data retrieval and analysis for a broad scientific community.