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

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.4K
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...
19.4K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.6K
14.6K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

375
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...
375
Protein Folding01:25

Protein Folding

10.7K
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...
10.7K
Protein Folding01:22

Protein Folding

125.6K
Overview
125.6K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

4.9K
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...
4.9K

You might also read

Related Articles

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

Sort by
Same author

Hsp110 mitigates α-synuclein pathology in vivo.

Proceedings of the National Academy of Sciences of the United States of America·2019
Same author

Transfer of pathogenic and nonpathogenic cytosolic proteins between spinal cord motor neurons in vivo in chimeric mice.

Proceedings of the National Academy of Sciences of the United States of America·2017
Same author

An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na<sup>+</sup>-Activated K<sup>+</sup> Channels in <i>Aplysia</i> Neurons.

The Journal of neuroscience : the official journal of the Society for Neuroscience·2017
Same author

Reduced high-frequency motor neuron firing, EMG fractionation, and gait variability in awake walking ALS mice.

Proceedings of the National Academy of Sciences of the United States of America·2016

Related Experiment Video

Updated: Dec 28, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.4K

Chaperonin-assisted protein folding: a chronologue.

Arthur L Horwich1,2, Wayne A Fenton2

  • 1Howard Hughes Medical Institute, Yale School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT06510, USA.

Quarterly Reviews of Biophysics
|February 20, 2020
PubMed
Summary

This review chronicles the discovery and development of chaperonins, protein machines that assist cellular protein folding. It details genetic, physiologic, biochemical, and biophysical studies of these ATP-utilizing molecular machines.

Keywords:
ChaperoninGroELGroESHsp60protein folding

More Related Videos

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

11.0K
Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

10.6K

Related Experiment Videos

Last Updated: Dec 28, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.4K
Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

11.0K
Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

10.6K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Chaperonins are essential molecular machines involved in protein folding within cells.
  • Understanding their structure and function is crucial for comprehending cellular proteostasis.

Purpose of the Study:

  • To document the historical discovery and scientific development of chaperonin research.
  • To provide a comprehensive overview of genetic, physiologic, biochemical, and biophysical studies on chaperonins.

Main Methods:

  • Chronological review of key experimental data and observations.
  • Integration of in vivo and in vitro findings.
  • Detailed illustration of pivotal experimental evidence.

Main Results:

  • Traces the evolution of knowledge regarding chaperonin structure, mechanism, and function.
  • Highlights the contributions of diverse experimental approaches to understanding these ATP-utilizing machines.

Conclusions:

  • Chaperonins play a vital role in assisting protein folding.
  • This chronologue offers a detailed historical perspective on their study, aiding researchers in navigating the field.