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

Genetic Drift

Genetic Drift

Natural selection—probably the most well-known evolutionary mechanism—increases the prevalence of traits that enhance survival and reproduction. However, evolution does not merely propagate favorable traits, nor does it always benefit populations.

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...

Gene Evolution - Fast or Slow?

Gene Evolution - Fast or Slow?

Conservation of Protein Domains

Conservation of Protein Domains

Protein Denaturation

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

You might also read

Related Articles

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

Sort by

Same author

Allosteric disordering of eIF2B regulates the integrated stress response.

Nature chemical biology·2026

Same author

Origins of allostery in vertebrate hemoglobin evolution.

bioRxiv : the preprint server for biology·2026

Same author

Design principles of a membrane-spanning ubiquitin ligase.

Molecular cell·2026

Same author

Conformational dynamics of SARS-CoV-2 spike on a membrane reveals the allosteric effects of furin cleavage and the D614G mutation.

Science advances·2026

Same author

Shapeshifting fungi: How morphological transitions can influence pathogenesis.

PLoS pathogens·2026

Same author

Epistatic drift in protein evolution.

Current opinion in genetics & development·2025

Same journal

The cell cloud: Adopting systems biology concepts in the era of single-cell immunology.

PLoS biology·2026

Same journal

Disinhibitory signaling enables flexible coding of top-down information in cortical networks.

PLoS biology·2026

Same journal

Correction: Cdc42 interacts with chaperone Ydj1 to enhance its stability and partitioning during asymmetric cell division and aging in yeast.

PLoS biology·2026

Same journal

Towards globally equitable bioinformatics adoption.

PLoS biology·2026

Same journal

The human claustrum supports cognitive networks for externally and internally driven task demands.

PLoS biology·2026

Same journal

Unusual decay: Recombination loss leads to splicing errors in green algae.

PLoS biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 21, 2026

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

Thermodynamic system drift in protein evolution.

Kathryn M Hart¹, Michael J Harms², Bryan H Schmidt³

¹Department of Chemistry, University of California, Berkeley, Berkeley, California, United States of America; Institute for Quantitative Biosciences (QB3), University of California, Berkeley, Berkeley, California, United States of America.

|November 12, 2014

Summary

This summary is machine-generated.

Bacterial ribonuclease H1 (RNH) proteins evolved diverse thermostabilities. Environmental selection drives overall stability, but evolutionary pathways explored varied mechanisms, a phenomenon termed "thermodynamic system drift."

More Related Videos

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Related Experiment Videos

Last Updated: Apr 21, 2026

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

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

Biochemistry
Evolutionary Biology
Structural Biology

Background:

Proteins from thermophiles are generally more thermostable than their mesophilic counterparts.
The evolutionary drivers of protein thermostability differences remain largely unknown.
Bacterial ribonuclease H1 (RNH) proteins from Thermus thermophilus (ttRNH) and Escherichia coli (ecRNH) exhibit a significant difference in melting temperature (T(m)) despite similar structures.

Purpose of the Study:

To investigate the evolutionary process underlying the diverse thermostabilities of bacterial RNH proteins.
To understand the relationship between environmental conditions and protein stability.
To explore the thermodynamic mechanisms driving changes in protein stability over evolutionary time.

Main Methods:

Characterization of RNH proteins from various extant bacteria.
Ancestral sequence reconstruction to infer evolutionary intermediates.
Synthesis and experimental characterization of ancestral RNH proteins, including measurement of thermodynamic parameters like heat capacity of unfolding (ΔCp).

Main Results:

RNH melting temperature (T(m)) correlates with species' growth temperatures, suggesting environmental selection.
Ancestral RNH proteins showed a gradual increase in T(m) along the ttRNH lineage and an abrupt decrease along the ecRNH lineage.
While T(m) changed smoothly, the underlying thermodynamic mechanisms (e.g., ΔCp) fluctuated, a phenomenon termed "thermodynamic system drift."

Conclusions:

Environmental selection is a strong driver for increased protein stability.
Proteins exhibit significant latitude in exploring sequence space and diverse stabilization mechanisms during evolution.
"Thermodynamic system drift" highlights the exploration of various biophysical strategies even under strong selective pressure.
This exploration of diverse mechanisms may open new evolutionary pathways.