Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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....

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Protein Modifications in the RER

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...

Protein Folding

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 Folding

Protein Folding

Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

You might also read

Related Articles

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

Sort by

Same author

From alkylating to shape-shifting G-quadruplex ligands: the RHAU peptide story.

Nucleic acids research·2026

Same author

Versatile introduction of multifunctional Michael-acceptor moieties on amino-oligonucleotides for bioconjugation purposes.

Communications chemistry·2026

Same author

Higher-Level Structural Classification of Pseudomonas Cyclic Lipopeptides through Their Bioactive Conformation.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2025

Same author

Profiling the Cellular Surfaceome by Furan-Based Protein Biotinylation.

Journal of proteome research·2025

Same author

Development of "Furan Warhead"-Equipped Antagonistic Nanobodies for Covalent Cross-Linking to the Epidermal Growth Factor Receptor.

Bioconjugate chemistry·2025

Same author

A short amphipathic peptide-based injectable hydrogel with antibacterial properties.

RSC advances·2025

Search research articles

Related Experiment Video

Updated: Mar 26, 2026

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

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

Published on: June 21, 2021

Chemical Protein Modification through Cysteine.

Smita B Gunnoo¹, Annemieke Madder²

¹Organic & Biomimetic Chemistry Research Group, Department of Organic and Macromolecular Chemistry, Ghent University, Krijgslaan 281, 9000, Gent, Belgium.

Chembiochem : a European Journal of Chemical Biology

|January 21, 2016

Summary

Chemically modifying proteins is crucial for many applications. This review highlights cysteine as an ideal amino acid for site-selective protein modification due to its unique chemical properties.

Keywords:

chemical protein modification cysteine proteins site-selectivity sulfur

More Related Videos

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

Related Experiment Videos

Last Updated: Mar 26, 2026

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

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

Published on: June 21, 2021

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

Area of Science:

Biochemistry
Chemical Biology
Protein Engineering

Background:

Protein modification is vital for diverse applications.
Achieving homogeneous, site-specific modification is challenging.
Random modification can lead to loss of protein function.

Purpose of the Study:

To review chemical protein modification strategies.
To highlight the advantages of using cysteine for site-selective modification.
To provide insights for researchers in protein chemistry.

Main Methods:

Targeting native cysteine residues.
Introducing cysteine via genetic engineering.
Utilizing cysteine's nucleophilicity and low abundance for selective reactions.

Main Results:

Cysteine offers chemo- and regioselectivity in protein modification.
Site-selective modification maintains protein homogeneity and function.
Cysteine-based strategies enable precise protein engineering.

Conclusions:

Cysteine is a superior amino acid for targeted chemical protein modification.
Genetic engineering combined with chemical methods allows precise protein functionalization.
This review serves as a guide for advancing protein modification techniques.