Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
15.0K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.6K
4.6K
Protein Networks02:26

Protein Networks

4.7K
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,...
4.7K
Protein Complex Assembly02:41

Protein Complex Assembly

17.1K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.1K
Protein Complex Assembly02:41

Protein Complex Assembly

2.7K
2.7K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
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...
3.1K

You might also read

Related Articles

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

Sort by
Same author

Authentic Phosphorylation of α-Synuclein at Ser129 Reveals Functional Differences Not Captured by the S129D Phosphomimetic.

ACS chemical biology·2026
Same author

Intracellular cyclization-coupled peptide library screening yields potent transcription factor antagonists.

Cell chemical biology·2026
Same author

InsiliCoil: An Integrated Software Suite for Coiled Coil Design, Prediction, and Therapeutic Engineering.

ACS synthetic biology·2025
Same author

Enhancing the Efficacy, Utility, and Throughput of the Transcription Block Survival Peptide Library Screening Platform.

JACS Au·2025
Same author

Stabilizing a Native Fold of Alpha-Synuclein with Short Helix-Constrained Peptides.

JACS Au·2025
Same author

An Intracellular Peptide Library Screening Platform Identifies Irreversible Covalent Transcription Factor Inhibitors.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2025

Related Experiment Video

Updated: Mar 28, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
08:38

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

Published on: March 3, 2015

14.0K

Deriving Heterospecific Self-Assembling Protein-Protein Interactions Using a Computational Interactome Screen.

Richard O Crooks1, Daniel Baxter1, Anna S Panek1

  • 1Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom.

Journal of Molecular Biology
|December 15, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed software to design specific protein-protein interactions (PPIs) using peptides. This method successfully created four pairs of heterospecific PPIs, enabling new applications in synthetic biology and disease modulation.

Keywords:
de novo designheterospecific proteinsinteractome screenpeptideprotein–protein interactions

More Related Videos

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

4.1K
A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

11.7K

Related Experiment Videos

Last Updated: Mar 28, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
08:38

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

Published on: March 3, 2015

14.0K
Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

4.1K
A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

11.7K

Area of Science:

  • Biochemistry
  • Computational Biology
  • Synthetic Biology

Background:

  • Naturally occurring protein-protein interactions (PPIs) are highly specific, and imbalances are linked to diseases.
  • Engineering specific designed protein-protein interactions (PPIs) remains a significant challenge.

Purpose of the Study:

  • To develop a computational approach for designing peptides that form specific heterospecific PPIs.
  • To accelerate the engineering of designed PPIs for various applications.

Main Methods:

  • Generated 1536 peptide sequences based on the parallel dimeric coiled-coil motif.
  • Screened a 1,180,416 member interactome for predicted melting temperatures (Tm).
  • Isolated eight peptides forming four heterospecific PPIs by applying predicted Tm cutoffs and disfavoring off-target interactions.

Main Results:

  • Successfully identified four pairs of heterospecific PPIs from the designed peptide library.
  • Verified the specificity of the four designed PPIs through characterization of all 36 possible pairs.
  • Refined the software by incorporating sequence filtering to remove antiparallel orientations.

Conclusions:

  • The developed computational approach effectively designs peptides for specific heterospecific PPIs.
  • This method allows for the derivation of complex sets of PPIs with potential applications in disease modulation, biomaterials, and synthetic biology.