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

9.9K
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....
9.9K
Protein Organization01:13

Protein Organization

160.2K
Overview
160.2K
Protein Folding01:22

Protein Folding

129.4K
Overview
129.4K
Protein Folding01:25

Protein Folding

12.0K
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...
12.0K
Protein and Protein Structure02:15

Protein and Protein Structure

90.8K
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...
90.8K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

14.9K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.9K

You might also read

Related Articles

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

Sort by
Same author

Forecasting left ventricular systolic dysfunction in heart failure with artificial intelligence.

EClinicalMedicine·2026
Same author

Artificial intelligence for hemodynamic monitoring with a wearable electrocardiogram monitor.

Communications medicine·2025
Same author

Effects of a diverse prebiotic fibre blend on inflammation, the gut microbiota and affective symptoms in metabolic syndrome: a pilot open-label randomised controlled trial.

The British journal of nutrition·2024
Same author

What is AI and why should I care?

Heart rhythm·2024
Same author

A Deep Learning Model for Inferring Elevated Pulmonary Capillary Wedge Pressures From the 12-Lead Electrocardiogram.

JACC. Advances·2024
Same author

Machine Learning for Risk Prediction: Does One Size Really Fit All?

JACC. Advances·2024

Related Experiment Video

Updated: Mar 7, 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

70.0K

Toward a consensus in protein structure nomenclature.

Linder C DaSilva1, Thomas Gurry2, Collin M Stultz3

  • 1Research Laboratory of Electronics; Massachusetts Institute of Technology; Cambridge, MA USA; ICET-CUAl Federal University of Mato Grosso; Barra do Garças, Brazil.

Intrinsically Disordered Proteins
|February 25, 2017
PubMed
Summary
This summary is machine-generated.

This study refines the nomenclature for intrinsically disordered proteins (IDPs). We propose an enhanced term to better capture the complex structural ensembles characteristic of these dynamic proteins.

Keywords:
intrinsically disordered proteinsnomenclatureorder parametersecondary structure

More Related Videos

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.7K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K

Related Experiment Videos

Last Updated: Mar 7, 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

70.0K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.7K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.8K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • A consensus nomenclature for intrinsically disordered proteins (IDPs) was recently proposed.
  • Existing terms for IDPs do not fully encompass their complex structural properties.
  • Proteins sampling diverse structures are crucial in biological processes.

Purpose of the Study:

  • To review and refine the nomenclature for intrinsically disordered proteins.
  • To propose a more nuanced descriptor for IDPs based on their ensemble of structures.
  • To enhance clarity and precision in scientific communication regarding IDPs.

Main Methods:

  • Systematic review of literature terms for disordered proteins.
  • Analysis of the ensemble of thermally accessible states for IDPs.
  • Comparative evaluation of nomenclature descriptors.

Main Results:

  • Agreement on "intrinsically disordered proteins" (IDPs) as a core descriptor.
  • Identification of limitations in current IDP nomenclature.
  • Proposal for a refined nomenclature accounting for structural ensembles.

Conclusions:

  • Refined nomenclature is essential for accurately describing IDPs.
  • Understanding the structural ensemble of IDPs is key to their functional characterization.
  • Improved terminology will advance research in intrinsically disordered proteins.