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

20.7K
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...
20.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.5K
15.5K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

690
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...
690
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.5K
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...
5.5K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

5.5K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.5K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

8.0K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
8.0K

You might also read

Related Articles

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

Sort by
Same author

[Diagnostic significance of ubiquitin C-terminal hydrolase L1 in patients with mine-blast traumatic brain injury].

Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova·2026
Same author

Advantages of aptamers as ligands upon protein detection by AFM-based fishing.

Analytical methods : advancing methods and applications·2025
Same author

Phylogenetic analysis of variants of the Puumala virus (Hantaviridae: <i>Orthohantavirus</i>) circulating in the Saratov region.

Voprosy virusologii·2024
Same author

Influence of Chaperones on Amyloid Formation of Аβ Peptide.

Current protein & peptide science·2022
Same author

Proteome data of serum samples from patients with schizophrenia.

Data in brief·2020
Same author

Verification of the Stabilized Protein Design Based on the Prediction of Intrinsically Disordered Regions: Ribosomal Proteins L1.

Biochemistry. Biokhimiia·2020

Related Experiment Video

Updated: Mar 25, 2026

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
07:14

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections

Published on: March 8, 2024

2.1K

Dataset concerning GroEL chaperonin interaction with proteins.

V V Marchenkov1, N Yu Marchenko1, A L Kaysheva1

  • 1Institute of Protein Research, RAS, Russia.

Data in Brief
|February 25, 2016
PubMed
Summary
This summary is machine-generated.

The GroEL chaperonin protein interacts with various native and denatured proteins in solution. This study also details using denatured pepsin for GroEL purification via affinity chromatography.

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

11.1K
Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

9.3K

Related Experiment Videos

Last Updated: Mar 25, 2026

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
07:14

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections

Published on: March 8, 2024

2.1K
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

11.1K
Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

9.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • The GroEL chaperonin is a crucial molecular machine involved in protein folding.
  • GroEL interacts with a diverse range of polypeptide chains, aiding in cellular protein homeostasis.

Purpose of the Study:

  • To investigate the interaction of GroEL chaperonin with native and denatured proteins in solution.
  • To demonstrate the utility of denatured pepsin in affinity chromatography for GroEL purification.

Main Methods:

  • Protein-protein interaction studies in solution.
  • Affinity chromatography utilizing immobilized denatured pepsin.
  • Analysis of GroEL binding to native (lysozyme, α-lactalbumin) and denatured (lysozyme, α-lactalbumin, pepsin) proteins.

Main Results:

  • GroEL exhibits interactions with both native and denatured forms of lysozyme, α-lactalbumin, and pepsin.
  • Affinity chromatography using denatured pepsin effectively purified GroEL, removing fluorescent impurities.

Conclusions:

  • GroEL chaperonin demonstrates broad substrate specificity, interacting with diverse protein conformations.
  • Denatured pepsin serves as an effective ligand for the purification of GroEL chaperonin through affinity chromatography.