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 Complex Assembly02:41

Protein Complex Assembly

16.9K
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...
16.9K
Protein Complex Assembly02:41

Protein Complex Assembly

2.6K
2.6K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.0K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
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...
3.0K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.2K
2.2K
Protein Organization01:24

Protein Organization

9.7K
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....
9.7K

You might also read

Related Articles

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

Sort by
Same author

Learning millisecond protein dynamics from what is missing in NMR spectra.

bioRxiv : the preprint server for biology·2026
Same author

Author Correction: De novo design of quasisymmetric two-component protein cages.

Nature·2026
Same author

Accurate protein stability prediction for small domains using mega-scale experiments.

bioRxiv : the preprint server for biology·2026
Same author

De novo design of quasisymmetric two-component protein cages.

Nature·2026
Same author

MX2 Mediates Collapse of the HIV-1 Capsid.

bioRxiv : the preprint server for biology·2026
Same author

Toward life with a 19-amino acid alphabet through generative artificial intelligence design.

Science (New York, N.Y.)·2026

Related Experiment Video

Updated: Feb 22, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.9K

Automatic structure prediction of oligomeric assemblies using Robetta in CASP12.

Hahnbeom Park1,2, David E Kim2,3, Sergey Ovchinnikov1,2

  • 1Department of Biochemistry, University of Washington, Seattle, Washington, 98195.

Proteins
|September 16, 2017
PubMed
Summary

We developed automated tools for predicting protein quaternary structures. Our method excelled in a blind test, accurately predicting symmetric protein assemblies and improving monomer structure prediction.

Keywords:
CASP12Rosettaprotein interfacesstructure predictionsymmetric assemblies

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

1.2K
Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.5K

Related Experiment Videos

Last Updated: Feb 22, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

69.9K
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

1.2K
Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.5K

Area of Science:

  • Structural biology
  • Computational biology
  • Biophysics

Background:

  • Many proteins function as symmetric assemblies, making quaternary structure prediction crucial.
  • Accurate prediction of these complex structures remains a significant challenge in molecular biology.

Purpose of the Study:

  • To present novel automated tools for predicting the quaternary structures of symmetric protein assemblies.
  • To evaluate the performance of these tools using data from the CASP12/CAPRI experiment.

Main Methods:

  • Development of automated computational tools integrated into the Robetta structure prediction server.
  • Assessment of the prediction pipeline on benchmark datasets, including CASP12/CAPRI targets.

Main Results:

  • Successfully predicted 5 out of 7 symmetric assemblies in the CASP12/CAPRI blind test.
  • Ranked as the top-performing server and one of two groups with high-quality predictions.
  • Demonstrated improved monomeric structure accuracy through oligomeric modeling, especially for intertwined structures.

Conclusions:

  • The developed automated tools are highly effective for predicting symmetric protein assemblies.
  • Oligomeric modeling offers a valuable strategy for enhancing protein structure prediction accuracy.