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 Folding01:25

Protein Folding

12.7K
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...
12.7K
Protein Folding01:22

Protein Folding

131.1K
Overview
131.1K
Protein Folding01:22

Protein Folding

36.7K
36.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

21.0K
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...
21.0K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.7K
15.7K
Protein Modifications in the RER01:26

Protein Modifications in the RER

7.6K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.6K

You might also read

Related Articles

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

Sort by
Same author

Fine-Tuning of the Endoplasmic Reticulum Stress Response Mechanism Plays a Key Role in Cellular Survival-A Mathematical Study.

International journal of molecular sciences·2025
Same author

Resveratrol-Supported Bioenergetics Leads to Higher Productivity and Accompanying Endoplasmic Reticulum Stress in a mAb-Producing CHO Cell Line.

International journal of molecular sciences·2025
Same author

Optimization of anion exchange chromatographic purification of adalimumab and evaluation of its combination with cation exchange method to improve purity.

Journal of pharmaceutical and biomedical analysis·2025
Same author

Research for a Common Thread: Insights into the Mechanisms of Six Potential Anticancer Agents.

Molecules (Basel, Switzerland)·2025
Same author

Fragility of ER homeostatic regulation underlies haploid instability in human somatic cells.

The Journal of biological chemistry·2024
Same author

The interlacing anticancer effect of pharmacologic ascorbate, chloroquine, and resveratrol.

BioFactors (Oxford, England)·2024

Related Experiment Video

Updated: Apr 12, 2026

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

Oxidative folding: recent developments.

András Szarka, Gábor Bánhegyi

    Biomolecular Concepts
    |May 12, 2015
    PubMed
    Summary

    Protein disulfide bond formation is key for protein structure and redox regulation. Recent research reveals new oxidizing compartments beyond the endoplasmic reticulum and periplasm, including the mitochondrial intermembrane space, and highlights regulatory roles for reversible disulfide bonds.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Protein Chemistry

    Background:

    • Disulfide bonds stabilize protein structure and regulate protein function through redox control.
    • Historically, the endoplasmic reticulum and prokaryotic periplasm were recognized as primary sites for disulfide bond formation.
    • Emerging evidence identifies new cellular compartments involved in protein oxidation.

    Purpose of the Study:

    • To review the current understanding of redox systems facilitating oxidative protein folding.
    • To highlight recent advancements in the field of disulfide bond formation.
    • To discuss the dual role of disulfide bonds in structure stabilization and redox regulation.

    Main Methods:

    • Literature review of recent scientific publications.

    More Related Videos

    Monitoring Equilibrium Changes in RNA Structure by 'Peroxidative' and 'Oxidative' Hydroxyl Radical Footprinting
    13:41

    Monitoring Equilibrium Changes in RNA Structure by 'Peroxidative' and 'Oxidative' Hydroxyl Radical Footprinting

    Published on: October 17, 2011

    14.7K
    Substructure Analyzer: A User-Friendly Workflow for Rapid Exploration and Accurate Analysis of Cellular Bodies in Fluorescence Microscopy Images
    14:28

    Substructure Analyzer: A User-Friendly Workflow for Rapid Exploration and Accurate Analysis of Cellular Bodies in Fluorescence Microscopy Images

    Published on: July 15, 2020

    8.5K

    Related Experiment Videos

    Last Updated: Apr 12, 2026

    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
    Monitoring Equilibrium Changes in RNA Structure by 'Peroxidative' and 'Oxidative' Hydroxyl Radical Footprinting
    13:41

    Monitoring Equilibrium Changes in RNA Structure by 'Peroxidative' and 'Oxidative' Hydroxyl Radical Footprinting

    Published on: October 17, 2011

    14.7K
    Substructure Analyzer: A User-Friendly Workflow for Rapid Exploration and Accurate Analysis of Cellular Bodies in Fluorescence Microscopy Images
    14:28

    Substructure Analyzer: A User-Friendly Workflow for Rapid Exploration and Accurate Analysis of Cellular Bodies in Fluorescence Microscopy Images

    Published on: July 15, 2020

    8.5K
  • Synthesis of current knowledge on protein redox systems.
  • Analysis of emerging findings on oxidative compartments and disulfide bond functions.

    • Main Results:

    • The mitochondrial intermembrane space is identified as a third major compartment for enzyme-mediated disulfide bond formation.
    • New observations are reshaping the understanding of oxidative folding mechanisms within the endoplasmic reticulum.
    • Reversible disulfide bridges in the endoplasmic reticulum are implicated in protein function regulation, beyond structural stabilization.

    Conclusions:

    • Protein oxidation is a more complex and widespread process than previously thought.
    • The mitochondrial intermembrane space represents a significant site for protein redox modifications.
    • Disulfide bond formation serves crucial roles in both protein structure and cellular signaling pathways.