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

13.5K
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...
13.5K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

3.9K
3.9K
Protein Networks02:26

Protein Networks

4.1K
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,...
4.1K
Structural Protein Function01:56

Structural Protein Function

2.8K
2.8K
Protein Organization01:24

Protein Organization

7.3K
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....
7.3K

You might also read

Related Articles

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

Sort by
Same author

Liquid-liquid phase separation enables chromatography-free purification and high-performance spidroin-amyloid hybrid silk fibers.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Membrane protein solubilization and structure determination using de novo-designed proteins.

Science (New York, N.Y.)·2026
Same author

Mass spectrometry integrates protein design into structural biology method development.

QRB discovery·2026
Same author

Allosteric targeting with antiviral nucleotide analogs allows fine-tuning of SAMHD1 dNTPase activity.

The Journal of biological chemistry·2026
Same author

Design of linear and cyclic peptide binders from protein sequence information.

Communications chemistry·2025
Same author

Chaperone-Mediated Regulation of Tau Phase Separation, Fibrillation, and Toxicity.

Journal of the American Chemical Society·2025

Related Experiment Video

Updated: Sep 18, 2025

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

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

18.2K

AI-first structural identification of pathogenic protein target interfaces.

Mihkel Saluri1, Michael Landreh1, Patrick Bryant2

  • 1Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Solna, Sweden.

Plos Computational Biology
|June 26, 2025
PubMed
Summary

Predicting protein structures reveals new human-pathogen interactions, accelerating vaccine and drug development. This study triples structural coverage, aiding the fight against infectious diseases.

More Related Videos

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

374
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.0K

Related Experiment Videos

Last Updated: Sep 18, 2025

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

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

18.2K
Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

374
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.0K

Area of Science:

  • Structural biology
  • Infectious disease research
  • Computational biology

Background:

  • Pandemic risk is rising due to increased global connectivity.
  • Understanding host-pathogen protein interactions is crucial for disease control.
  • Existing structural data for these interactions is severely limited (0.2%).

Purpose of the Study:

  • To explore the structural protein-protein interaction network between humans and ten pathogens.
  • To leverage advanced protein structure prediction for host-pathogen interactions.
  • To identify novel structural targets for therapeutic and vaccine development.

Main Methods:

  • Utilized AlphaFold and homology modeling for structure prediction.
  • Investigated 9,452 human-pathogen interactions, focusing on those with unknown structures.
  • Employed native mass spectrometry for experimental validation.

Main Results:

  • Predicted structures for 9,452 interactions, significantly expanding coverage.
  • Identified 30 high-confidence interactions (TM-score ≥0.9), tripling existing structural data.
  • Confirmed a novel heterotetrameric complex involving Francisella tularensis and human IGKC.

Conclusions:

  • Protein structure prediction is a powerful tool for host-pathogen interaction studies.
  • The identified interactions offer new targets for drug and vaccine design.
  • Findings pave the way for rapid advancement in combating emerging infectious diseases.