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

Bacterial Protein Maturation01:26

Bacterial Protein Maturation

48
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
48
Responses to Heat and Cold Stress02:45

Responses to Heat and Cold Stress

13.6K
Every organism has an optimum temperature range within which healthy growth and physiological functioning can occur. At the ends of this range, there will be a minimum and maximum temperature that interrupt biological processes.
13.6K
Diversity of Archaea IV01:29

Diversity of Archaea IV

64
Hyperthermophilic archaea are a group of extremophiles thriving at temperatures above 80°C, often in hydrothermal vents and volcanic soils where conditions surpass the boiling point of water. At such temperatures, proteins, membranes, and DNA in most organisms degrade, but hyperthermophiles have evolved remarkable adaptations to maintain stability and function.Unique Cellular FeaturesHyperthermophilic membranes are composed of a monolayer of biphytanyl tetraether lipids, which resist...
64
Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

37
Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
37
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.1K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.1K
Protein Denaturation01:28

Protein Denaturation

4.4K
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...
4.4K

You might also read

Related Articles

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

Sort by
Same author

Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Interpretable machine learning uncovers structural determinants of Wnt-Wntless binding specificity from atomistic simulations.

Communications chemistry·2026
Same author

STI1 domain engages transient helices to mediate Dsk2 phase separation and proteasome condensation.

The EMBO journal·2026
Same author

Water-mediated hydrogen bonds and local side-chain interactions in the cooperative collapse and expansion of PNIPAM oligomers.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Erratum: YAP condensates are highly organized hubs.

iScience·2026
Same author

Single-Particle Emission Microscopy of Green-Emitting Carbon Dots Made from Top-Down and Bottom-Up Precursors.

The journal of physical chemistry letters·2025

Related Experiment Video

Updated: Aug 7, 2025

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

6.2K

TMAO: Protecting proteins from feeling the heat.

Mayank M Boob1, Shahar Sukenik2, Martin Gruebele3

  • 1Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois.

Biophysical Journal
|March 14, 2023
PubMed
Summary

Trimethylamine N-oxide (TMAO) enhances protein thermal stability by favoring compact structures. TMAO forms hydration shells that stabilize proteins, with effects saturating at 1M concentration.

More Related Videos

Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

14.2K
Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

3.6K

Related Experiment Videos

Last Updated: Aug 7, 2025

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

6.2K
Intracellular Refolding Assay
07:18

Intracellular Refolding Assay

Published on: January 24, 2012

14.2K
Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

3.6K

Area of Science:

  • Biochemistry
  • Biophysics
  • Computational Biology

Background:

  • Osmolytes like TMAO are crucial for cellular protein stability under stress.
  • TMAO protects marine life from pressure denaturation, but its thermal protection is unquantified.
  • Understanding TMAO's role in thermal stabilization is key to cellular resilience.

Purpose of the Study:

  • To quantify the effect of TMAO on protein thermal stability.
  • To investigate TMAO's influence on protein folding ensembles and hydration shells at varying temperatures.
  • To elucidate the molecular mechanisms of TMAO-mediated thermal protection.

Main Methods:

  • All-atom molecular dynamics simulations (>190 μs) of a model protein (PRB) at multiple temperatures and TMAO concentrations.
  • Analysis of protein folding/unfolding dynamics and hydration shell structure.
  • Examination of TMAO-protein and TMAO-water interactions.

Main Results:

  • TMAO significantly increases the thermal stability of the model protein PRB.
  • Partly structured, compact protein ensembles are favored over the unfolded state in the presence of TMAO.
  • TMAO forms distinct inner and outer hydration shells around the protein, altering water dynamics and increasing hydration.
  • The stabilizing effect of TMAO saturates at approximately 1M concentration.

Conclusions:

  • TMAO effectively stabilizes proteins against thermal denaturation through a cooperative hydration shell mechanism.
  • The saturation of TMAO's effect suggests limited evolutionary pressure for extremophiles to accumulate very high intracellular concentrations.
  • These findings provide molecular insights into osmolyte function and protein adaptation to environmental stress.