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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
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
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.

You might also read

Related Articles

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

Sort by
Same author

Secretin-interacting plug proteins prevent antibiotic influx during type IV pilus assembly in Pseudomonas aeruginosa.

Nature communications·2026
Same author

Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.

Nature chemical biology·2026
Same author

Peroxidasin enables melanoma immune escape by inhibiting natural killer cell cytotoxicity.

Molecular oncology·2026
Same author

Pervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRC.

Science signaling·2026
Same author

Identification of receptor-binding domains of Bacteroidales antibacterial pore-forming toxins.

The Journal of biological chemistry·2025
Same author

Single-cell imaging of liver metabolic dynamics using fluorescent biosensors.

Trends in endocrinology and metabolism: TEM·2025

Related Experiment Video

Updated: Jun 8, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

How proteins form disulfide bonds.

Matthieu Depuydt1, Joris Messens, Jean-Francois Collet

  • 1de Duve Institute, Université catholique de Louvain, Brussels, Belgium.

Antioxidants & Redox Signaling
|September 21, 2010
PubMed
Summary

This review covers oxidative protein folding, the process of forming native disulfide bonds in proteins. It summarizes known pathways in bacteria, eukaryotes, and mitochondria, highlighting remaining challenges.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein disulfide isomerase discovery initiated the study of oxidative protein folding.
  • Oxidative protein folding is crucial for native protein structure and function.
  • Disulfide bond formation pathways are essential cellular processes.

Purpose of the Study:

  • To review current knowledge on disulfide bond formation pathways.
  • To compare oxidative folding mechanisms across different cellular compartments and organisms.
  • To identify unresolved problems in the field of disulfide bond formation.

Main Methods:

  • Literature review of scientific publications on oxidative protein folding.
  • Synthesis of information on disulfide bond formation pathways in prokaryotes and eukaryotes.

More Related Videos

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Related Experiment Videos

Last Updated: Jun 8, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

  • Comparative analysis of identified pathways and mechanisms.

    • Main Results:

    • Detailed description of disulfide bond formation pathways in bacterial periplasm (DsbA-DsbD), endoplasmic reticulum (PDI, Ero1), and mitochondrial intermembrane space (Mia40, Erv1).
    • Elucidation of the roles of key proteins in each pathway.
    • Identification of conserved and distinct features of oxidative folding across different systems.

    Conclusions:

    • Significant progress has been made in understanding disulfide bond formation.
    • Key proteins and pathways involved in oxidative folding are identified.
    • Major challenges and future research directions in oxidative protein folding remain.