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 Folding01:22

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
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

You might also read

Related Articles

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

Sort by
Same author

Effects of Probe-Related Correlations on Local Electrostatic Potentials Around DNA.

Journal of computational chemistry·2025
Same author

Murine norovirus allosteric escape mutants mimic gut activation.

Journal of virology·2025
Same author

Strong field gradients enable NMR-based diffusion measurements for K<sup>+</sup>, Mg<sup>2+</sup>, Cl<sup>-</sup>, and SO<sub>4</sub><sup>2-</sup> ions in biomolecular solutions.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2025
Same author

The need to implement FAIR principles in biomolecular simulations.

Nature methods·2025
Same author

Murine norovirus allosteric escape mutants mimic gut activation.

bioRxiv : the preprint server for biology·2025
Same author

Peptide diffusion in biomolecular condensates.

Biophysical journal·2024

Related Experiment Video

Updated: Jun 18, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Osmolyte solutions and protein folding.

Char Y Hu1, B Montgomery Pettitt, Joerg Roesgen

  • 1Chemistry Department, University of Houston, Houston, TX 77204-5003, USA.

F1000 Biology Reports
|December 5, 2009
PubMed
Summary
This summary is machine-generated.

Osmolytes are natural compounds that stabilize proteins by altering their folding. This review examines experimental, theoretical, and simulation findings on osmolyte mechanisms in protein stability.

More Related Videos

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Related Experiment Videos

Last Updated: Jun 18, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Osmolytes are vital intracellular compounds.
  • They play a crucial role in maintaining protein stability under stress.
  • Understanding their function is key to cellular homeostasis.

Purpose of the Study:

  • To review the evolving understanding of osmolytes' role in protein stability.
  • To explore the mechanisms by which osmolytes influence protein folding.
  • To integrate experimental, theoretical, and simulation perspectives.

Main Methods:

  • Literature review of recent research.
  • Analysis of experimental data on protein-ligand interactions.
  • Evaluation of theoretical models and molecular simulations.

Main Results:

  • Osmolytes modulate the protein folding landscape.
  • Specific mechanisms involve preferential hydration and direct osmolyte-protein interactions.
  • Experimental and simulation results align with current theories.

Conclusions:

  • Osmolytes are essential regulators of protein structure and function.
  • A comprehensive understanding requires integrating diverse research approaches.
  • Further research will refine our knowledge of osmolyte-mediated protein stabilization.