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Related Concept Videos

Covalently Linked Protein Regulators02:04

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.
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Protein Modifications in the RER01:26

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 sequences.
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Jun 7, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Chemoenzymatic methods for site-specific protein modification.

David Rabuka1

  • 1Redwood Bioscience, Burlingame, CA 94010, USA. drabuka@redwoodbioscience.com

Current Opinion in Chemical Biology
|October 30, 2010
PubMed
Summary

Chemists are developing new ways to modify proteins precisely using chemical tags and enzymes. This chemoenzymatic approach allows for site-specific protein engineering and novel applications in biotechnology.

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Protein Engineering

Background:

  • Traditional protein modification methods lack selectivity.
  • Achieving site-specific protein modification is challenging due to complex chemical environments.
  • Novel chemical handles are needed for precise protein functionalization.

Purpose of the Study:

  • To review advancements in chemoenzymatic techniques for protein modification.
  • To highlight methods for generating protein-small molecule constructs.
  • To showcase novel applications of site-specific protein engineering.

Main Methods:

  • Introduction of unique chemical handles (tags) into target proteins.
  • Selective and irreversible enzymatic modification of these tags.

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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

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

Related Experiment Videos

Last Updated: Jun 7, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

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

  • Engineering enzymes to tolerate substrate analogs for modified protein generation.
  • Chemoenzymatic synthesis of protein-small molecule conjugates.
  • Main Results:

    • Development of orthogonal chemical handles for site-specific protein modification.
    • Successful chemoenzymatic generation of engineered proteins.
    • Demonstration of diverse applications for chemically modified proteins.
    • Progress in creating protein-small molecule constructs with high precision.

    Conclusions:

    • Chemoenzymatic strategies offer precise control over protein modification.
    • Site-specific protein engineering is advancing rapidly.
    • These methodologies enable novel applications in biotechnology and beyond.