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

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids02:04

Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

5.7K
Diols are compounds with two hydroxyl groups. In addition to syn dihydroxylation, diols can also be synthesized through the process of anti dihydroxylation. The process involves treating an alkene with a peroxycarboxylic acid to form an epoxide. Epoxides are highly strained three-membered rings with oxygen and two carbons occupying the corners of an equilateral triangle. This step is followed by ring-opening of the epoxide in the presence of an aqueous acid to give a trans diol.
5.7K
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

9.9K
Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.
9.9K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.1K
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...
5.1K
Preparation of Epoxides03:00

Preparation of Epoxides

7.5K
Overview
Epoxides result from alkene oxidation, which can be achieved by a) air, b) peroxy acids, c) hypochlorous acids, and d) halohydrin cyclization.
Epoxidation with Peroxy Acids
Epoxidation of alkenes via oxidation with peroxy acids involves the conversion of a carbon–carbon double bond to an epoxide using the oxidizing agent meta-chloroperoxybenzoic acid, commonly known as MCPBA. Since the O–O bond of peroxy acids is very weak, the addition of electrophilic oxygen of...
7.5K
Acid-Catalyzed Ring-Opening of Epoxides02:24

Acid-Catalyzed Ring-Opening of Epoxides

7.2K
Epoxides that are three-membered ring systems are more reactive than other cyclic and acyclic ethers. The high reactivity of epoxides originates from the strain present in the ring. This ring strain acts as a driving force for epoxides to undergo ring-opening reactions either with halogen acids or weak nucleophiles in the presence of mild acid. The acid catalyst converts the epoxide oxygen, a poor leaving group, into an oxonium ion, a better leaving group, making the reaction feasible. The...
7.2K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.8K

You might also read

Related Articles

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

Sort by
Same author

High-Yield Production and Cost-Effective Purification of an Alkali-Resistant Hexameric Protein A Variant for Antibody Affinity Chromatography.

Biotechnology journal·2026
Same author

Bioinspired Antimicrobial Strategy: An Extremophile Deep Sea Peptide to Combat Cystic Fibrosis Infections Caused by <i>Pseudomonas aeruginosa</i> and <i>Staphylococcus aureus</i>.

Marine drugs·2026
Same author

Site-Specific Antigen Immobilization Improves Autoantibody Binding Efficiency on the Luminex Platform.

ACS omega·2026
Same author

Computational design of a single-chain galectin-1 yields a stable variant with retained glycan binding activity.

Journal of biotechnology·2026
Same author

Directed Functionalization of Recombinant Spider Silk Nonwoven Membranes with Antibodies Using Non-Canonical Amino Acids.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

A Robust Bioprocess for the Global Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts Produces Labeled Proteins at the Gram Scale.

Chembiochem : a European journal of chemical biology·2025

Related Experiment Video

Updated: Jun 12, 2025

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry
12:31

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry

Published on: August 19, 2012

24.3K

Protocol for protein modification using oxalyl thioester-mediated chemoselective ligation.

Francesco Terzani1, Chen Wang1, Simindokht Rostami2

  • 1Université de Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017, Center for Infection and Immunity of Lille, 59000 Lille, France.

STAR Protocols
|October 16, 2024
PubMed
Summary

This study introduces a novel oxalyl thioester precursor (oxoSEA) for fast, site-specific protein modification. The method enables efficient protein labeling using native chemical ligation, advancing chemical biology tools.

Keywords:
ChemistryMolecular/Chemical ProbesProtein Biochemistry

More Related Videos

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

1.7K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.7K

Related Experiment Videos

Last Updated: Jun 12, 2025

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry
12:31

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry

Published on: August 19, 2012

24.3K
Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

1.7K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.7K

Area of Science:

  • Chemical Biology
  • Organic Chemistry
  • Biochemistry

Background:

  • Site-specific protein modification is crucial for chemical biology.
  • Fast and efficient ligation chemistries are in high demand.
  • Existing methods may have limitations in speed or specificity.

Purpose of the Study:

  • To describe the preparation of a novel oxalyl thioester precursor, the oxoSEA group.
  • To detail the incorporation of this precursor into peptide modifiers via solid-phase peptide synthesis.
  • To demonstrate the application of this method for site-specific protein modification using native chemical ligation.

Main Methods:

  • Preparation of an N-oxalyl perhydro-1,2,5-dithiazepine handle (oxoSEA).
  • Incorporation of the oxoSEA group into a peptide modifier using solid-phase peptide synthesis.
  • Application of the modified peptide for native chemical ligation with a cysteine-containing protein domain.

Main Results:

  • Successful synthesis of the oxoSEA precursor.
  • Efficient incorporation of the oxoSEA group into peptide modifiers.
  • Demonstrated site-specific modification of a streptococcal G protein B1 domain.

Conclusions:

  • The developed oxalyl thioester precursor (oxoSEA) offers a fast and efficient method for site-specific protein modification.
  • This protocol facilitates protein labeling through native chemical ligation.
  • The study provides a valuable new tool for chemical biology research.