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

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

7.3K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
7.3K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.7K
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....
7.7K
Histone Modification02:32

Histone Modification

14.5K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
14.5K

You might also read

Related Articles

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

Sort by
Same author

Naked antisense oligonucleotides remain endolysosomally sequestered despite induced membrane damage.

bioRxiv : the preprint server for biology·2026
Same author

Traceless protein semisynthesis in cells using the promiscuous ultra-fast split intein NrdJ-1.

Chemical science·2026
Same author

Population-level analysis of glycoprotein glycoforms.

mAbs·2026
Same author

Traceless protein semi-synthesis in cells using the promiscuous ultra-fast split intein NrdJ-1.

bioRxiv : the preprint server for biology·2026
Same author

The Role of Glycan Structures in Modulating GM-CSF Bioactivity: Insights from Glycoengineering.

bioRxiv : the preprint server for biology·2026
Same author

Click-Cyclized Cell Penetrating Peptides Containing Hydrophobic Proline Derivatives for Efficient Intracellular Delivery.

Angewandte Chemie (International ed. in English)·2025

Related Experiment Video

Updated: Oct 5, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

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

Published on: December 9, 2017

7.1K

Highly Selective Lysine Acylation in Proteins Using a Lys-His Tag Sequence.

Christian Kofoed1,2, Shunliang Wu1, Kasper K Sørensen1

  • 1Department of Chemistry, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|January 31, 2022
PubMed
Summary

Introducing Lys-His tags for highly selective protein acylation. This method enables precise modification of lysine residues, expanding applications in bioconjugation and therapeutic development.

Keywords:
acylationantibodieschemical biologypeptide tagssite-selective protein modification

More Related Videos

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.1K
Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

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

Published on: April 4, 2018

11.8K

Related Experiment Videos

Last Updated: Oct 5, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

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

Published on: December 9, 2017

7.1K
Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

4.1K
Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

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

Published on: April 4, 2018

11.8K

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Protein Engineering

Background:

  • Chemical modification of proteins is crucial for diverse applications.
  • Achieving high selectivity for lysine modification remains a challenge.
  • Previous work demonstrated N-terminal His tags for selective Nα-amine acylation.

Purpose of the Study:

  • To develop a method for selective acylation of lysine Nε-amines.
  • To introduce Lys-His tags for targeted protein modification.
  • To demonstrate the versatility and applicability of the Lys-His tag system.

Main Methods:

  • Design and synthesis of Lys-His peptide tags (Hisn-Lys-Hism).
  • Incorporation of Lys-His tags into proteins at various sites (C-terminus, loops).
  • Acylation of tagged proteins using simple acylating agents under mild conditions.

Main Results:

  • Lys-His tags facilitate highly selective acylation of the designated Lys Nε-amine.
  • Modification occurs under mild conditions with high selectivity over native lysine residues.
  • The method was successfully applied to acylate the therapeutic antibody Rituximab, even in mixed protein samples.

Conclusions:

  • Lys-His tags offer a flexible and efficient strategy for site-specific protein acylation.
  • This method overcomes previous selectivity challenges in protein modification.
  • The technology holds significant potential for bioconjugation, antibody modification, and therapeutic development.