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 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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Protein Organization01:13

Protein Organization

Overview
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

SPPIDER-seq: sequence-based partner-aware predictor of protein-protein interaction sites.

Bioinformatics (Oxford, England)·2026
Same author

BPabZIP, a new bZIP protein motif that promotes binding near, and displacement of, nucleosomes.

bioRxiv : the preprint server for biology·2026
Same author

Single-cell RNA sequencing defines developmental progression and reproductive transitions of <i>Pneumocystis carinii</i>.

Microbiology spectrum·2025
Same author

Catalytic region mimetics in Na+/H+ exchanger regulatory factor 4 suppress guanylate cyclase 2C activity to regulate enterotoxin triggered diarrhea.

The Journal of biological chemistry·2025
Same author

Case Report: Association of Ocular Colobomas With a Novel Missense Variant in CDC42, a Member of the Rho Family of Small GTPases.

Clinical genetics·2025
Same author

Role of Forkhead box F1 in the Pathobiology of Pulmonary Arterial Hypertension.

bioRxiv : the preprint server for biology·2024

Related Experiment Video

Updated: Jul 12, 2026

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy
08:30

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D.

Aleksey Porollo1, Jaroslaw Meller

  • 1Department of Environmental Health, University of Cincinnati, Cincinnati, OH 45267, USA. alexey.porollo@uc.edu

BMC Bioinformatics
|August 31, 2007
PubMed
Summary

POLYVIEW-3D is a new web server that enhances protein structure analysis through advanced visualization and annotation. It simplifies creating publication-quality images and animations of protein complexes for research and education.

More Related Videos

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Related Experiment Videos

Last Updated: Jul 12, 2026

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy
08:30

Visualization of Recombinant DNA and Protein Complexes Using Atomic Force Microscopy

Published on: July 18, 2011

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

  • Structural Bioinformatics
  • Molecular Biology
  • Computational Chemistry

Background:

  • Macromolecular visualization and automated annotation are crucial for understanding molecular systems in the post-genomic era.
  • Three-dimensional (3D) models aid in identifying drug targets and functionally important regions of proteins.
  • Advanced tools are needed to integrate databases, annotation servers, and rendering programs for comprehensive analysis.

Purpose of the Study:

  • To present POLYVIEW-3D, a novel web tool for protein structure analysis, focusing on annotation and visualization of protein complexes.
  • To extend the capabilities of the previously developed POLYVIEW web server.
  • To provide a user-friendly interface for generating high-quality visualizations and annotations.

Main Methods:

  • Integration of web technology with state-of-the-art macromolecular visualization software (PyMol).
  • Development of a platform-independent web server requiring no plug-ins.
  • Implementation of versatile structural and functional annotation options for protein complexes.

Main Results:

  • POLYVIEW-3D enables the creation of publication-quality structure renderings and animated images.
  • The server facilitates detailed structural and functional analysis, particularly for protein-protein interactions.
  • Examples demonstrating the utility of POLYVIEW-3D for various annotation options are provided.

Conclusions:

  • The POLYVIEW-3D server offers high-quality macromolecular structure presentation via PyMol rendering and an intuitive web interface.
  • It provides extensive automated structural and functional analysis capabilities for proteins and their complexes.
  • POLYVIEW-3D is a valuable resource for researchers and educators in protein science and structural bioinformatics.