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

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

Conservation of Protein Domains Over Different Proteins

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...

Gene Evolution - Fast or Slow?

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

Conservation of Protein Domains

Signal Sequences and Sorting Receptors

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

Mutation, Gene Flow, and Genetic Drift

Mutation, Gene Flow, and Genetic Drift

In a population that is not at Hardy-Weinberg equilibrium, the frequency of alleles changes over time. Therefore, any deviations from the five conditions of Hardy-Weinberg equilibrium can alter the genetic variation of a given population. Conditions that change the genetic variability of a population include mutations, natural selection, non-random mating, gene flow, and genetic drift (small population size).

You might also read

Related Articles

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

Sort by

Same author

A quantitative comparison of the deleteriousness of missense and nonsense mutations using the structurally resolved human protein interactome.

Protein science : a publication of the Protein Society·2025

Same author

Effect of Protein-Polarized Ligand Charges on Relative Protein Ligand Binding Affinities.

Journal of chemical theory and computation·2024

Same author

Are transient protein-protein interactions more dispensable?

PLoS computational biology·2022

Same author

Haplotype-resolved de novo assembly of the Vero cell line genome.

NPJ vaccines·2021

Same author

Quantifying evolutionary importance of protein sites: A Tale of two measures.

PLoS genetics·2021

Same author

A reference map of the human binary protein interactome.

Nature·2020

Search research articles

Related Experiment Video

Updated: Sep 18, 2025

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

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

Published on: July 14, 2015

The Impact of Disorder-Order Switching on Protein Sequence Evolution.

Avital Sharir-Ivry¹, Yu Xia¹

¹Department of Bioengineering, McGill University, Montreal, QC H3A 0E9, Canada.

|June 23, 2025

Summary

Proteins switching between disordered and ordered states evolve slowly, facing strong evolutionary pressure. This conservation extends to the entire protein, including ordered regions, due to coupled folding and binding requirements.

More Related Videos

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

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

Published on: February 10, 2023

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Published on: February 3, 2023

Related Experiment Videos

Last Updated: Sep 18, 2025

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

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

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

Published on: February 10, 2023

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Published on: February 3, 2023

Area of Science:

Evolutionary biology
Structural biology
Biochemistry

Background:

Protein structure dictates protein evolution at the residue level.
Proteins with multiple conformations present challenges in understanding structure-evolution relationships.
Previously, proteins switching between native states showed stronger selective pressure.

Purpose of the Study:

Analyze residue-level evolutionary rates for proteins with disorder-order switching regions in the yeast proteome.
Investigate the impact of disorder-order transitions on protein evolutionary rates.
Compare evolutionary rates of disorder-order switching proteins with other protein types.

Main Methods:

Analysis of evolutionary rates at the residue level.
Focus on proteins exhibiting disorder-order switching regions within the yeast proteome.
Comparative analysis with structured proteins and conformational switches.

Main Results:

Proteins with disorder-order switching regions evolve significantly slower than structured proteins.
These proteins experience even slower evolution than conformational switches.
Selective pressure affects the entire protein, conserving ordered residues more than in structured proteins.
Disordered regions capable of switching to ordered states are highly conserved.

Conclusions:

The need to encode and maintain coupled folding and binding imposes unique, strong selective pressure on the entire protein.
Disorder-order switching regions are under significant evolutionary constraint.
These findings offer insights into the evolution of intrinsically disordered proteins and their functions.