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

Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...
Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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 Folding01:22

Protein Folding

Overview

You might also read

Related Articles

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

Sort by
Same author

Individualised N-terminal Pro-B-type Natriuretic Peptide Thresholds for the Diagnosis of Heart Failure: A Proof-of-Concept Study.

Cureus·2026
Same author

Circulating Endotrophin Predicts Myocardial Fibrosis Burden and Is Sensitive to Antifibrotic Therapy.

JACC. Advances·2026
Same author

Domain-specific mechanisms of YAP1 variants in ocular coloboma revealed by in-vitro and organoid studies.

Biochimica et biophysica acta. Molecular basis of disease·2026
Same author

Structural Constraints Acting on the SARS-CoV-2 Spike Protein Reveal Limited Space for Viral Adaptation.

Genome biology and evolution·2026
Same author

Characterising the heterogeneity of heart failure with preserved ejection fraction: moving beyond subgroups and distinguishing disease from risk.

European journal of heart failure·2026
Same author

Overcoming Hyperkalaemia as a Barrier to Achieving Optimal RAASi Therapy and Cardiorenal Protection in Individuals with Cardiorenal Disease: A Podcast Discussion.

Advances in therapy·2026
Same journal

Population Epigenetics: Deciphering DNA Methylation Diversity and its Implications for Health, Disease, and Evolution.

Molecular biology and evolution·2026
Same journal

Genomic signature of repeated transitions to diurnality in spiders.

Molecular biology and evolution·2026
Same journal

Phylogenomic blind spots: The limits of UCE and BUSCO loci in the presence of gene flow.

Molecular biology and evolution·2026
Same journal

seqLens: Optimizing Language Models for Genomic Predictions.

Molecular biology and evolution·2026
Same journal

The transcriptional and translational outcomes for pseudogenes in bacterial endosymbionts.

Molecular biology and evolution·2026
Same journal

800 million years of co-evolution in the green plant lineage - the case of LEUNIG and SEUSS transcriptional co-regulators.

Molecular biology and evolution·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 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

The effect of sequence evolution on protein structural divergence.

Simon G Williams1, Simon C Lovell

  • 1Faculty of Life Sciences, University of Manchester, Manchester, UK.

Molecular Biology and Evolution
|February 6, 2009
PubMed
Summary
This summary is machine-generated.

Protein evolution involves both sequence changes and structural adjustments. This study reveals that proteins accommodate mutations through coevolution and by altering their structure, offering a unified view of molecular evolution.

More Related Videos

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

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
16:02

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

Published on: February 10, 2023

Related Experiment Videos

Last Updated: Jun 25, 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

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

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
16:02

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

Published on: February 10, 2023

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Protein structure and function impose complex evolutionary constraints.
  • Analyzing sequence differences in homologous proteins aids understanding of structural divergence and evolutionary rules.

Purpose of the Study:

  • To assess the relationship between amino acid sequence and structural divergence in proteins.
  • To investigate the evolutionary mechanisms governing protein sequence and structural changes.

Main Methods:

  • Analysis of sequence differences between homologous proteins.
  • Assessment of evolutionary constraints such as solvent exposure and secondary structure.
  • Identification and analysis of radical size-changing mutations and their compensatory or mitigating mechanisms.

Main Results:

  • Protein sequence-structural divergence is influenced by evolutionary constraints like solvent exposure and secondary structure.
  • Many radical size-changing mutations are not compensated by neighboring changes.
  • Noncompensated substitutions are mitigated by alterations in protein structure.

Conclusions:

  • Proteins accommodate substitutions through a combined mechanism of coevolution and structural accommodation.
  • This dual mechanism explains correlated substitutions distant in sequence and structure.
  • Provides an integrated perspective on protein sequence and structural divergence during evolution.