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.

You might also read

Related Articles

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

Sort by

Same author

Synthesis of DNA-Encoded Libraries by Tryptophan-Selective Bioconjugation.

Organic letters·2026

Same author

Catalytic strategies for post-translational modifications regulating protein higher-order structure and properties.

Chemical Society reviews·2026

Same author

Electron Donor-Acceptor (EDA) Complex Formation via Spatial Control of Donor-Acceptor Interactions.

The Journal of organic chemistry·2025

Same author

Azaanthraquinone PCET Catalysis Enables Chemoselective Decarboxylative Functionalization of Diverse Carboxylic Acids.

Journal of the American Chemical Society·2025

Same author

Visible light-driven stereodivergent allylation of cyclic hemiacetals with butene for polypropionate synthesis.

Science (New York, N.Y.)·2025

Same author

A reflection on ketoABNO: the crossing point between organic synthesis and protein modification.

Chemical science·2025

Same journal

Pressure-Related Challenges and Strategic Approaches in Lithium Metal Sulfide all-Solid-State Batteries.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Dual Regulatory Functions of Classical Zinc Finger Clusters from Myeloid Zinc Finger-1.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

A Selectfluor-based Polonovski Rearrangement Leading to Novel Entities for Synthetic and Medicinal Applications.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Relay Approach: A Convergent Synthesis of Key Fragments en route to (+)-Neosorangicin A.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Working Under Pressure: Empirical Findings on the Challenges Facing PhD Students in Chemistry.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Charge Resonance Interaction in Aromatic Trimer Radical Cations Revealed by IR Spectroscopy: The Case of Pyrrole Homo- and Heterotrimers.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: May 31, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

Precision Chemistry for Protein Lysine Modification.

Mayu Onoda¹, Motomu Kanai¹

¹Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|May 30, 2026

Summary

This summary is machine-generated.

Studying lysine post-translational modifications (PTMs) is vital for understanding cellular signaling. New ligand-guided catalysis offers precise, programmable control over lysine modification, advancing synthetic epigenetics research.

Keywords:

catalysis epigenetics lysine post‐translational modifications regioselectivity

More Related Videos

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Related Experiment Videos

Last Updated: May 31, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Area of Science:

Biochemistry
Chemical Biology
Molecular Biology

Background:

Lysine post-translational modifications (PTMs) are critical regulators of protein function, structure, and cellular signaling pathways.
Studying PTMs requires homogeneous proteins with site-specific modifications, which is challenging due to the similar chemistry and variable reactivity of lysine residues.
Existing chemical methods for lysine modification are often limited in scope and selectivity, especially for less accessible sites.

Purpose of the Study:

To develop advanced chemical strategies for achieving regioselective and catalytic modification of lysine residues.
To create a platform for the precise installation of authentic PTMs on proteins.
To enable programmable control over lysine modification for applications in synthetic epigenetics.

Main Methods:

Exploiting enzymatic principles of substrate recognition and spatial organization to guide chemical reactions.
Developing ligand-directed chemistry and proximity-enabled modification strategies.
Utilizing on-demand generation of highly reactive electrophiles for targeted modifications.
Advancing ligand-guided catalysis for selective lysine modification.

Main Results:

Demonstrated regioselective and catalytic installation of biorelevant, authentic PTMs.
Developed a versatile platform for programmable lysine modification.
Overcame limitations of earlier chemical strategies for modifying sterically hindered or low-reactivity lysine sites.

Conclusions:

Ligand-guided catalysis represents a significant advancement in achieving precise control over lysine PTMs.
This approach provides a powerful tool for synthetic epigenetics and detailed functional studies of PTMs.
The developed platform facilitates the generation of homogeneous, site-specifically modified proteins for various biological investigations.