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 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.
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Simulation of cell-size systems at long timescales with flexible protein structures.

bioRxiv : the preprint server for biology·2026
Same author

Insulin modulates mPFC gene expression and emotional behavior in a sex-specific manner following fetal growth restriction.

Brain, behavior, and immunity·2026
Same author

Prenatal metabolic adversity reprograms insulin-responsive transcription in the developing nucleus accumbens.

Molecular metabolism·2026
Same author

SENSAAS-Bioisostere: A computational method for 3D shape-guided bioisosteric replacements and scaffold-hopping.

European journal of medicinal chemistry·2026
Same author

Astrocyte fatty acid metabolism as a driver of risk for major depressive disorder.

Nature communications·2026
Same author

Genome-wide methylation patterns associated with chronic stress.

Epigenomics·2026

Related Experiment Video

Updated: Jul 2, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Large-scale structural modeling of protein complexes at low resolution.

Zhengwei Zhu1, Andrey Tovchigrechko, Tatiana Baronova

  • 1Center for Bioinformatics, The University of Kansas, 2030 Becker Drive, Lawrence, KS 66047, USA.

Journal of Bioinformatics and Computational Biology
|September 4, 2008
PubMed
Summary

We developed a new method to predict protein complex structures using genome-wide protein interaction data. This approach enhances our understanding of molecular life processes by modeling protein interactions at scale.

More Related Videos

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

Related Experiment Videos

Last Updated: Jul 2, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

Area of Science:

  • Structural biology
  • Bioinformatics
  • Systems biology

Background:

  • Understanding protein-protein interactions is crucial for elucidating molecular mechanisms of life.
  • Genome-wide studies provide vast datasets of protein interactions but often lack structural information.
  • Predicting the structure of protein complexes is essential for functional and mechanistic insights.

Purpose of the Study:

  • To develop and implement a computational methodology for predicting protein complex structures at a genome-wide scale.
  • To integrate experimental protein interaction data with protein structure prediction.
  • To create a comprehensive database resource for accessing predicted protein complex structures.

Main Methods:

  • Utilized the protein docking approach (GRAMM) combined with the DOCKGROUND resource of experimentally determined protein-protein structures.
  • Developed a full sequence-to-structure-of-complex modeling pipeline.
  • Implemented the pipeline within the Genome Wide Docking Database (GWIDD) resource, importing and unifying data from external interaction networks.

Main Results:

  • Successfully predicted structures for a large number of protein complexes from genome-wide interaction data.
  • Created the Genome Wide Docking Database (GWIDD) as a centralized resource.
  • Enabled retrieval or modeling of individual protein structures and prediction of complex structures.

Conclusions:

  • The developed methodology and GWIDD resource facilitate the study of protein-protein interactions at a systems level.
  • This approach provides valuable structural insights into molecular life processes.
  • GWIDD offers a user-friendly web interface for accessing comprehensive protein sequence, structure, and docking information.