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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 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,...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Related Experiment Video

Updated: Jun 21, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Using peptide array to identify binding motifs and interaction networks for modular domains.

Shawn S-C Li1, Chenggang Wu

  • 1Department of Biochemistry and the Siebens-Drake Medical Research Institute, Schulich School of Medicine and Dentistry, University of Western Ontario, London, ON, Canada.

Methods in Molecular Biology (Clifton, N.J.)
|August 4, 2009
PubMed
Summary

High-density peptide arrays effectively map protein-protein interactions by identifying specific peptide motifs recognized by modular domains like Src-homology 2 (SH2) and Src-homology 3 (SH3). This technology reveals cellular signaling networks.

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Last Updated: Jun 21, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

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Published on: November 18, 2014

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Proteomics

Background:

  • Protein-protein interactions are fundamental to cellular processes and signal transduction.
  • Modular domains recognizing short linear peptide sequences are common in macromolecular recognition.
  • The human genome encodes numerous peptide-binding domains, highlighting the significance of this interaction mode.

Purpose of the Study:

  • To demonstrate the utility of high-density peptide arrays for mapping protein-protein interaction networks.
  • To showcase the application of peptide arrays in identifying specific motifs recognized by SH2 domains.
  • To illustrate the use of peptide arrays in uncovering SH3 domain-mediated interaction networks.

Main Methods:

  • Utilizing high-density peptide array libraries to screen for binding interactions.
  • Employing oriented peptide array libraries to identify specific motifs for domains like SH2.
  • Applying complementary biochemical assays alongside peptide arrays.

Main Results:

  • Successfully identified specific motifs recognized by an SH2 domain using oriented peptide arrays.
  • Uncovered interaction networks mediated by the SH3 domain through high-density peptide arrays.
  • Demonstrated the broad applicability of these methods to other modular and catalytic domains.

Conclusions:

  • High-density peptide arrays are powerful tools for dissecting domain-mediated protein-protein interactions.
  • These methods enable proteome-level mapping of interaction networks.
  • The described techniques can be extended to study various modular domains involved in peptide recognition.