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 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,...
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,...
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...

You might also read

Related Articles

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

Sort by
Same author

Lentiviral SgRNA Delivery for CRISPR/Cas9 Editing in Cre-Dependent Cas9 Knock-in Primary Mouse Hepatocytes.

Journal of visualized experiments : JoVE·2026
Same author

A Scalable, Direct-to-Biology Platform for Accelerated Discovery of Cereblon-Based Molecular Glue Degraders.

Angewandte Chemie (International ed. in English)·2026
Same author

RIPK3 Orchestrates Scar-Associated Macrophage Dysfunction to Drive Pulmonary Fibrosis.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

A Rapid, High-Throughput Method for the Construction of Mutagenesis Libraries.

Biomolecules·2025
Same author

Systematic optimization of prime editing for enhanced efficiency and versatility in genome engineering across diverse cell types.

Frontiers in cell and developmental biology·2025
Same author

Author Correction: SGF29 nuclear condensates reinforce cellular aging.

Cell discovery·2025

Related Experiment Video

Updated: Jun 18, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Library-based, multiplexed strategy for mapping protein interaction networks via crosslinking.

Yuxin Lu1,2, Shuting Meng3, Yi Zhang1,2

  • 1School of Chinese Materia Medica, Nanjing University of Chinese Medicine, Nanjing, China.

BMC Biotechnology
|June 17, 2026
PubMed
Summary

This study introduces a new method using mutagenesis libraries to map protein interactions, identifying novel partners for PSMD10 and advancing proteasome interactome research.

Keywords:
Amber codon scanningCrosslinking mass spectrometryPhoto-crosslinkingProtein-protein interactionsScanning mutagenesis library

More Related Videos

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Related Experiment Videos

Last Updated: Jun 18, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Protein-protein interactions are crucial for cellular processes but difficult to study, especially weak or transient ones.
  • Traditional methods using noncanonical amino acids have limitations in coverage and identifying interaction hotspots.

Purpose of the Study:

  • To develop a high-coverage strategy for mapping protein interaction interfaces in situ.
  • To identify novel interaction partners and binding sites of the PSMD10 protein.

Main Methods:

  • Constructed an amber codon-scanning mutagenesis library for PSMD10.
  • Incorporated the photocrosslinking noncanonical amino acid (ncAA) p-azido-phenylalanine at multiple sites.
  • Utilized crosslinking mass spectrometry (XL-MS) for interaction analysis.

Main Results:

  • Successfully mapped multiple interaction regions on PSMD10 with broad coverage.
  • Identified previously unreported interaction partners, including T2FA, TBA1C, and ATRIP.
  • Revealed specific residues involved in intermolecular interactions.

Conclusions:

  • Expanded understanding of the PSMD10-associated proteasome interactome.
  • Demonstrated a multiplexed strategy for in situ mapping of protein interaction interfaces.
  • Provided a platform for developing therapeutics targeting protein-protein interactions.