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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites01:49

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...
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...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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,...

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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

SH3 domain protein-binding arrays.

Sangpen Chamnongpol1, Xianqiang Li

  • 1Panomics, Redwood City, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 17, 2004
PubMed
Summary
This summary is machine-generated.

This study introduces a high-throughput assay for visualizing protein-protein interactions involving Src Homology 3 (SH3) domains. The method uses immobilized SH3 domain proteins for rapid, cost-effective analysis of intercellular communication and signal transduction pathways.

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Last Updated: Jun 21, 2026

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Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

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Identification of Modified Histones as Binding Substrates of Human Spindlin Family Member 4 (SPIN4) by Peptide Arrays and Native Nucleosome Pulldown
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cellular Biology

Background:

  • Src Homology 3 (SH3) domains are crucial for intercellular communication and intracellular signal transduction.
  • SH3 domains were first identified as part of the Rous sarcoma oncogene product Src.

Purpose of the Study:

  • To develop a high-throughput assay for analyzing ligand binding to SH3 domains.
  • To enable rapid visualization of numerous SH3 domain protein-protein interactions.

Main Methods:

  • Utilizes SH3 domain proteins immobilized on a membrane array.
  • Involves cloning a protein of interest into a fusion-tagged expression vector and expressing it in bacteria.
  • Incubates bacterial extract with the array membrane and detects signals using chemiluminescence.

Main Results:

  • The assay allows for rapid visualization of SH3 domain protein-protein interactions.
  • Requires no expensive equipment or radioactivity.
  • The procedure is straightforward once the array is constructed or obtained.

Conclusions:

  • This high-throughput assay provides a cost-effective and efficient method for studying SH3 domain interactions.
  • Facilitates research in intercellular communication and signal transduction.