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

Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

Ligand Binding and Linkage

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...

Tagging and Fusion Proteins

Tagging and Fusion Proteins

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...

You might also read

Related Articles

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

Sort by

Same author

Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.

Angewandte Chemie (International ed. in English)·2026

Same author

TAV2b Peptide Derivatives Underwind and Stabilize Double-Stranded RNA upon Binding.

Journal of the American Chemical Society·2026

Same author

LetA defines a structurally distinct transporter family.

Nature·2026

Same author

Stabilizing Proteins by Chemical Cross-Linking: Insights into Conformation, Unfolding, and Aggregation Using Native Ion Mobility Mass Spectrometry.

Analytical chemistry·2025

Same author

Temporal and Spatial Characterization of CUL3<sup>KLHL20</sup>-Driven Targeted Degradation of BET Family BRD Proteins by the Macrocycle-Based Degrader BTR2004.

ACS chemical biology·2025

Same author

β-Hairpin Peptidomimetics for Protein-Protein Interaction Inhibition.

Methods in molecular biology (Clifton, N.J.)·2025

Search research articles

Related Experiment Video

Updated: May 2, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Protein-templated peptide ligation.

Nicolas Brauckhoff¹, Gernot Hahne, Johannes T-H Yeh

¹Chemical Genomics Centre of the Max Planck Society, Otto-Hahn-Strasse 15, 44227 Dortmund (Germany).

Angewandte Chemie (International Ed. in English)

|March 20, 2014

Summary

This summary is machine-generated.

Researchers developed the first protein-templated reaction for N-terminal peptide ligation. This method significantly accelerates reactions, showing promise for applications like protein labeling in complex biological samples.

Keywords:

bioorthogonal reactions peptide ligation protein modification solid-phase peptide synthesis templated reactions

More Related Videos

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

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

Published on: February 5, 2020

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Related Experiment Videos

Last Updated: May 2, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

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

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

Published on: February 5, 2020

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

Biochemistry
Chemical Biology
Molecular Biology

Background:

Molecular templates enhance reaction rates by concentrating reactants.
Nucleic acid templated reactions are well-established.
Protein-based molecular recognition is crucial in biological systems.

Purpose of the Study:

To introduce the first protein-templated chemical reaction.
To enable N-terminal linkage of two peptides using a protein scaffold.
To demonstrate the utility of protein-templated reactions in biological contexts.

Main Methods:

Utilized a protein scaffold to orient and ligate two peptides at their N-termini.
Quantified reaction rate acceleration using the protein template compared to untemplated reactions.
Tested the reaction's selectivity and robustness in crude cell lysate for protein labeling.

Main Results:

Achieved acceleration of peptide ligation by over three orders of magnitude with the protein template.
Demonstrated high selectivity for the N-terminal ligation of peptides.
Successfully applied the protein-templated ligation for labeling proteins in crude cell lysate.

Conclusions:

Protein-templated reactions represent a novel strategy for accelerating chemical transformations.
This method provides a highly efficient and selective approach for peptide ligation.
The demonstrated robustness in cell lysate highlights potential applications in bioconjugation and chemical biology.