Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein and Protein Structure

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 Organization

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

Machine Learning Reveals the Contribution of Rare Genetic Variants and Enhances Risk Prediction for Coronary Artery Disease in the Japanese Population.

Circulation. Genomic and precision medicine·2026

Same author

Impact of small area-level deprivation on survival outcomes in patients with Cholangiocarcinoma: a population-based multilevel survival analysis.

Frontiers in public health·2026

Same author

Missing Occupation, Missing Risk: Insights From COVID-19 Case Investigation Data in Busan, South Korea.

Journal of preventive medicine and public health = Yebang Uihakhoe chi·2026

Same author

Seroprevalence and Epidemiological Characteristics of Severe Fever with Thrombocytopenia Syndrome in Patients with Chronic Diseases in Korea.

Viruses·2026

Same author

Nationwide seroprevalence of severe fever with thrombocytopenia syndrome virus in South Korea: Regional patterns and public health implications.

Ticks and tick-borne diseases·2026

Same author

Li<sub>1+<i>x</i></sub>TaO<sub><i>x</i></sub>F<sub>6-<i>x</i></sub> Oxyfluoride Solid Electrolytes with Amorphization-Driven Enhancement of Ion Conduction Channels for 5 V All-Solid-State Batteries.

Journal of the American Chemical Society·2026

Same journal

Research on multi-trait genome association study method based on Shannon information entropy.

BMC bioinformatics·2026

Same journal

A multi-view feature fusion framework with interpretable graph convolution for predicting microbe-drug associations.

BMC bioinformatics·2026

Same journal

Covariance decomposition for distance based species tree estimation.

BMC bioinformatics·2026

Same journal

SNPio: a Python interface for population genomic data processing.

BMC bioinformatics·2026

Same journal

SpaHNR: a spatial domain identification method via sparse attention-based hierarchical node representation and multi-view contrastive learning.

BMC bioinformatics·2026

Same journal

OpenIMC: an open-source platform for analyzing single-cell and spatial proteomics by imaging mass cytometry.

BMC bioinformatics·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Detecting internally symmetric protein structures.

Changhoon Kim¹, Jodi Basner, Byungkook Lee

¹Laboratory of Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bldg 37, Room 5120, 37 Convent Dr MSC 4264, Bethesda, MD 20892-4264, USA.

BMC Bioinformatics

|June 8, 2010

Summary

This summary is machine-generated.

A new method called SymD can detect internally symmetric proteins by comparing a protein structure to its circularly permuted copies. This method estimates that 10-15% of proteins are symmetric, offering insights into protein folding and evolution.

More Related Videos

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

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

Published on: July 17, 2019

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Related Experiment Videos

Last Updated: Jun 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

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

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

Published on: July 17, 2019

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Area of Science:

Structural biology
Bioinformatics
Protein science

Background:

Many functional proteins exhibit symmetric structures, either as multimeric complexes or within monomeric states.
Internally symmetric proteins are significant for understanding protein folding, function, and evolution.
Existing detection algorithms often overlook symmetry information, focusing instead on repeating structural units.

Purpose of the Study:

To introduce a novel method, SymD, for identifying internally symmetric protein structures.
To analyze the prevalence and types of symmetry in protein domains.

Main Methods:

The SymD method compares a protein structure against circularly permuted versions of itself.
This approach is robust against symmetry-breaking insertions and deletions.
It effectively amplifies symmetry signals for accurate detection.

Main Results:

SymD successfully identifies 70-80% of TIM barrel domains and 100% of beta-propellers as symmetric.
The procedure estimates that 10-15% of proteins in the ASTRAL 40 database possess internal symmetry.
Symmetric proteins are found across all structural classes, exhibiting diverse architectures.

Conclusions:

SymD is a sensitive tool for detecting internal protein symmetry.
An estimated 10-15% of known protein domains are internally symmetric.
The study provides an overview of the diversity of symmetries and folds in protein structures.