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

8.7K
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...
8.7K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
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...
3.8K
Protein and Protein Structure02:15

Protein and Protein Structure

81.4K
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...
81.4K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.6K
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...
5.6K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

88
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...
88
Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation01:22

Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation

380
Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
380

You might also read

Related Articles

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

Sort by
Same author

Construction of <i>ortho</i>-C-N Bond and <i>ipso</i>-C(sp<sup>2</sup>)-C(sp<sup>3</sup>) Bond by Amination/Decarboxylation Catellani Reaction.

Organic letters·2026
Same author

Efficacy and implementation of digital health interventions in chronic kidney disease: an umbrella review of systematic evidence.

Kidney research and clinical practice·2026
Same author

Temperature Range Thermal Proteome Profiling for Drug Target Identification: A Practical Guide.

Journal of proteome research·2026
Same author

PlanarFold: a coarse-grained molecular dynamics model of RNA in two-dimensional space.

Nature communications·2026
Same author

FOXM1 modulates keloid fibroblast proliferation and migration via the BMP4/Smad1/5/8 axis.

Burns : journal of the International Society for Burn Injuries·2026
Same author

Pore Wall Engineered Covalent-Organic Frameworks as Size-Matched Nanotraps Enable Highly Selective Adsorption of Sulfonamide Antibiotics.

Environmental science & technology·2026

Related Experiment Video

Updated: Sep 13, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.4K

Glutathione Regulating Aggregation and Depolymerization Mechanism of Whey Protein Isolate.

Yuzhi Tian1, Zhishen Mu2, Sinan Mu1

  • 1Key Laboratory of Dairy Science (Northeast Agricultural University), Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin, 150030, China.

Journal of Agricultural and Food Chemistry
|July 28, 2025
PubMed
Summary

Glutathione (GSH) affects whey protein isolate (WPI) aggregation and depolymerization. Higher GSH concentrations depolymerized WPI, while specific concentrations induced aggregation and cross-linking, impacting food applications.

Keywords:
aggregation−depolymerization mechanismchemical cross-linking coupled with mass spectrometryglutathioneheating temperaturewhey protein isolate

More Related Videos

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

3.0K
Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.1K

Related Experiment Videos

Last Updated: Sep 13, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.4K
Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

3.0K
Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.1K

Area of Science:

  • Food Science
  • Protein Chemistry
  • Biochemistry

Background:

  • Whey protein isolate (WPI) is a valuable food ingredient.
  • Understanding protein aggregation is crucial for food processing and functionality.
  • Glutathione (GSH) is a known bioactive thiol compound.

Purpose of the Study:

  • To investigate the impact of varying glutathione (GSH) concentrations on whey protein isolate (WPI) aggregation and depolymerization.
  • To elucidate the molecular mechanisms underlying GSH-WPI interactions at different temperatures.
  • To identify specific cross-linking sites formed during GSH-induced WPI modification.

Main Methods:

  • Investigated WPI aggregation/depolymerization across a range of GSH concentrations (0-60 mM) and temperatures (50, 65, 80 °C).
  • Measured molecular weight, particle size, absolute potential, and endogenous fluorescence of WPI-GSH complexes.
  • Utilized Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC/MS/MS) to identify cross-linked peptides.

Main Results:

  • GSH induced depolymerization of WPI aggregates at 50 and 80 °C, decreasing molecular weight and particle size.
  • At 65 °C, GSH initially increased WPI aggregation before causing depolymerization.
  • LC/MS/MS identified novel intermolecular, intramolecular, and cyclic cross-linked peptides, with specific sites on alpha-lactalbumin and beta-lactoglobulin identified.

Conclusions:

  • GSH concentration and temperature significantly influence WPI aggregation and depolymerization through thiol-disulfide exchange reactions.
  • Specific GSH concentrations (2-10 mM) promote aggregation, while higher concentrations (20-60 mM) lead to depolymerization.
  • This study provides molecular insights into GSH's role in modulating whey protein structure, relevant for food industry applications.