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 Folding01:25

Protein Folding

8.8K
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...
8.8K
Protein Folding01:22

Protein Folding

112.3K
Overview
112.3K
Protein Folding01:22

Protein Folding

29.8K
29.8K
Protein Organization01:13

Protein Organization

123.4K
Overview
123.4K
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

You might also read

Related Articles

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

Sort by
Same author

Protocadherin-1 deficiency increases baseline and allergen-induced airway hyperresponsiveness in mice.

American journal of respiratory cell and molecular biology·2026
Same author

Disease-associated genetic variants can cause missense effects in tissue-specific protein isoforms.

Nature communications·2026
Same author

Heterogeneity and dynamics of DENV-specific CD8 + T cells in dengue infection.

Nature communications·2026
Same author

A Hormone Cell Atlas maps the human endocrine system at cellular resolution.

Science (New York, N.Y.)·2026
Same author

An integrated single-cell and spatial proteotranscriptomics atlas of fibroblast-driven immunoregulation within the human adult oral cavity.

Cell press blue·2026
Same author

Decoding Human T Cell Immunity with Artificial Intelligence and Single-Cell Genomics.

Annual review of immunology·2026

Related Experiment Video

Updated: May 5, 2026

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

16.2K

Parallel dynamics and evolution: Protein conformational fluctuations and assembly reflect evolutionary changes in

Joseph A Marsh1, Sarah A Teichmann

  • 1European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, UK.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|November 26, 2013
PubMed
Summary
This summary is machine-generated.

Protein structure and evolution are both dynamic processes. This review highlights how changes in protein sequence and structure are linked to flexibility, motions, and assembly, offering insights into function.

Keywords:
assembly pathwayintrinsically disordered proteinsprotein complex assemblyprotein dynamicsprotein flexibilityquaternary structure

More Related Videos

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

1.2K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K

Related Experiment Videos

Last Updated: May 5, 2026

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

16.2K
Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

1.2K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.2K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Proteins exhibit dynamic structural changes, including conformational fluctuations and assembly into complexes.
  • Protein families show significant evolutionary variations in structure across different levels (secondary, tertiary, quaternary).
  • Recent research indicates parallels between structural dynamics and evolutionary changes in proteins.

Purpose of the Study:

  • To review evidence linking protein evolutionary changes to structural dynamics.
  • To explore the role of local flexibility, large-scale motions, and quaternary structure assembly in evolution.
  • To discuss how neutral evolution explains these correspondences and how deviations offer functional insights.

Main Methods:

  • Review of existing literature and experimental evidence.
  • Analysis of correlations between protein sequence/structure variations and dynamic properties.
  • Integration of concepts from structural biology, molecular evolution, and biophysics.

Main Results:

  • Evolutionary changes in protein sequence and structure are closely associated with local flexibility, disorder, large-scale motions, and quaternary structure assembly.
  • Neutral evolution provides a framework for understanding many of these observed correspondences.
  • Deviations from these correspondences highlight specific functional adaptations.

Conclusions:

  • The relationship between protein structure, dynamics, function, and evolution is intimate and interconnected.
  • Understanding these dynamics offers insights into protein adaptation and functional innovation.
  • Future research and practical applications can leverage this integrated perspective.