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

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-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,...
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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

You might also read

Related Articles

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

Sort by
Same author

Structural Analysis of Valine Residues in Silk Fibroin by Solid-State NMR.

Journal of the American Chemical Society·2025
Same author

Agent-based modelling of the early stages of actin polymerisation required to drive endocytosis in Saccharomyces cerevisiae.

Scientific reports·2025
Same author

Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation.

Communications biology·2025
Same author

Improvement in protein HSQC spectra from addition of betaine.

Journal of biomolecular NMR·2025
Same author

Corrigendum to "Dissecting the Enterococcal Polysaccharide Antigen (EPA) structure to explore innate immune evasion and phage specificity" [Carbohydr. Polym. 347 (1 January 2025) 122686].

Carbohydrate polymers·2024
Same author

Dissecting the Enterococcal Polysaccharide Antigen (EPA) structure to explore innate immune evasion and phage specificity.

Carbohydrate polymers·2024
Same journal

TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosis.

Biochemical Society transactions·2026
Same journal

Advancing the monitoring of organelle contact sites in vitro and in vivo.

Biochemical Society transactions·2026
Same journal

Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.

Biochemical Society transactions·2026
Same journal

Replication associated nuclear DNA mismatch repair across kingdoms.

Biochemical Society transactions·2026
Same journal

Phosphatases of regenerating liver downregulate PTEN to promote tumorigenesis.

Biochemical Society transactions·2026
Same journal

Implications of Rho GTPase signaling in cancer immunotherapy.

Biochemical Society transactions·2026
See all related articles

Related Experiment Video

Updated: Jun 10, 2026

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Protein-protein interactions.

Mike P Williamson1, Michael J Sutcliffe

  • 1Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK. m.williamson@sheffield.ac.uk

Biochemical Society Transactions
|July 28, 2010
PubMed
Summary
This summary is machine-generated.

High-throughput methods like two-hybrid screens and tandem affinity purification (TAP) tagging identify protein complexes. These studies reveal complex structures and the existence of metabolons, though metabolons remain elusive to high-throughput detection due to potential fragility.

More Related Videos

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

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

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Related Experiment Videos

Last Updated: Jun 10, 2026

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

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

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

  • Proteomics
  • Biochemistry
  • Systems Biology

Background:

  • Protein complexes are fundamental to cellular function.
  • High-throughput methods are crucial for mapping protein interactions and complex organization.
  • The structure of protein complexes, including core and peripheral proteins, is key to understanding their roles.

Purpose of the Study:

  • To describe standard high-throughput methods for protein complex identification.
  • To review the characterization of the Saccharomyces cerevisiae interactome using these methods.
  • To discuss the existence and detection challenges of metabolons.

Main Methods:

  • Two-hybrid screens for identifying protein-protein interactions.
  • Tandem affinity purification (TAP) tagging for isolating protein complexes.
  • Analysis of interactome data to determine protein complex composition.

Main Results:

  • The majority of proteins in Saccharomyces cerevisiae exist within complexes.
  • Protein complexes often feature a stable core with associated 'party' and 'dater' proteins.
  • Metabolons, complexes of enzymes in the same metabolic pathway, are proposed but not detected by current high-throughput assays.

Conclusions:

  • High-throughput methods have significantly advanced our understanding of protein complex organization.
  • The fragility of metabolons may explain their absence in high-throughput studies.
  • Further investigation is needed to develop methods for detecting labile complexes like metabolons.