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Related Concept Videos

Peptide Bonds02:43

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...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Related Experiment Video

Updated: May 28, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Click to join peptides/proteins together.

Xuechen Li1

  • 1Department of Chemistry, The University of Hong Kong, Hong Kong, China. xuechenl@hku.hk

Chemistry, an Asian Journal
|November 2, 2011
PubMed
Summary
This summary is machine-generated.

Copper-catalyzed azide-alkyne cycloaddition (CuAAC) enables efficient peptide and protein modification. This click chemistry creates triazole linkages that mimic natural peptide bonds, facilitating synthetic protein and peptidomimetic design.

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Identifying Protein-protein Interaction Sites Using Peptide Arrays
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Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

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Last Updated: May 28, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Chemical Biology

Background:

  • Copper(I) catalyzes Huisgen 1,3-dipolar cycloaddition reactions.
  • The copper-catalyzed azide-alkyne cycloaddition (CuAAC) is a highly selective "click" reaction.
  • CuAAC is tolerant to diverse pH and solvent conditions, suitable for biomolecule conjugation.

Purpose of the Study:

  • To review the scope and applications of CuAAC in peptide and protein chemistry.
  • To highlight the utility of CuAAC for creating peptidomimetics and synthetic proteins.
  • To explore the potential of triazole linkages as peptide bond mimics.

Main Methods:

  • Copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) reaction.
  • Ligation of peptides and proteins.
  • Synthesis of triazole-backbone-modified peptides.

Main Results:

  • CuAAC proceeds with excellent chemoselectivity under various conditions.
  • The reaction yields a 1,4-disubstituted-1,2,3-triazole moiety.
  • Triazole linkages exhibit properties similar to natural peptide bonds, including hydrogen bonding and conformational restriction.

Conclusions:

  • CuAAC is a powerful tool for synthetic peptide and protein chemistry.
  • Triazole-backbone modification allows for the creation of peptides with native-like secondary structures.
  • This methodology facilitates the development of novel peptidomimetics and synthetic proteins.