Jove
Visualize
Contact Us

Related Concept Videos

Protein Organization01:13

Protein Organization

123.3K
Overview
123.3K
Protein Organization01:24

Protein Organization

7.2K
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....
7.2K
Protein Organization01:24

Protein Organization

9.0K
9.0K
Protein Organization01:13

Protein Organization

19.5K
19.5K
Protein and Protein Structure02:15

Protein and Protein Structure

71.5K
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...
71.5K
Protein Folding01:22

Protein Folding

112.3K
Overview
112.3K

You might also read

Related Articles

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

Sort by
Same author

Airway epithelial cells and macrophages trigger IL-6-CD95/CD95L axis and mediate initial immunopathology of COVID-19.

iScience·2023
Same author

Plasma Sphingomyelin Disturbances: Unveiling Its Dual Role as a Crucial Immunopathological Factor and a Severity Prognostic Biomarker in COVID-19.

Cells·2023
Same author

The Significance of Hypervariability and Conserved Motifs in Antimicrobial Peptides from Tree Frogs.

Journal of natural products·2023
Same author

The Interplay among Glucocorticoid Therapy, Platelet-Activating Factor and Endocannabinoid Release Influences the Inflammatory Response to COVID-19.

Viruses·2023
Same author

The turning point of COVID-19 severity is associated with a unique circulating neutrophil gene signature.

Immunology·2023
Same author

Celastrol: A lead compound that inhibits SARS-CoV-2 replication, the activity of viral and human cysteine proteases, and virus-induced IL-6 secretion.

Drug development research·2022
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 Experiment Video

Updated: May 3, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

7.1K

Extended secondary structures in proteins.

Léo Degrève, Carlos A Fuzo, Antonio Caliri

    Biochimica Et Biophysica Acta
    |February 12, 2014
    PubMed
    Summary

    Extended secondary structures (ESSs) are common in globular proteins, stabilizing protein structures. These fused secondary structures involve about 30% of residues, enhancing conformational stability and protein folding.

    Area of Science:

    • Protein structure and folding
    • Structural bioinformatics
    • Biophysics

    Background:

    • Super secondary structures are known but often overlooked beyond basic identification.
    • Deeper fusion of secondary structures in globular proteins requires further investigation.

    Purpose of the Study:

    • To demonstrate that associated secondary structures sharing backbone residues, termed extended secondary structures (ESSs), are common in globular proteins.
    • To investigate the role of ESSs in stabilizing secondary and tertiary protein structures.

    Main Methods:

    • Statistical analysis of 163 randomly selected proteins from the Protein Data Bank.
    • Detailed structural analysis of specific protein cases.
    • Molecular Dynamics (MD) simulations of protein-aqueous solvent systems to analyze ESS stability.

    More Related Videos

    Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
    07:26

    Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

    Published on: November 21, 2013

    12.4K
    Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
    14:55

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

    Published on: September 17, 2017

    16.8K

    Related Experiment Videos

    Last Updated: May 3, 2026

    Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
    11:14

    Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

    Published on: January 6, 2017

    7.1K
    Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
    07:26

    Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

    Published on: November 21, 2013

    12.4K
    Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
    14:55

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

    Published on: September 17, 2017

    16.8K

    Main Results:

    • Approximately 30% of residues in a protein participate in ESS on average.
    • MD simulations showed high conformational stability for ESSs, indicated by narrow root mean squared deviation distributions.
    • ESSs form stable aggregates that significantly enhance protein conformational stability.

    Conclusions:

    • Extended secondary structures (ESSs) are a ubiquitous and specific feature in globular proteins.
    • ESSs play a crucial role in stabilizing protein structures and may be involved in domain formation.
    • Further research into the function and significance of ESSs in protein architecture is warranted.