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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...
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...
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 Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: Jun 17, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
13:42

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Peptoid-Peptide hybrid backbone architectures.

Christian A Olsen1

  • 1Department of Medicinal Chemistry, University of Copenhagen, Universitetsparken 2, Copenhagen, 2100 Denmark. cao@farma.ku.dk caolsen@scripps.edu

Chembiochem : a European Journal of Chemical Biology
|December 18, 2009
PubMed
Summary

This review surveys hybrid peptidomimetics, focusing on alpha/beta-peptides and peptoids. It highlights research on mixed backbones combining alpha-amino acids and N-alkylglycine oligomers.

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Last Updated: Jun 17, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
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Area of Science:

  • Peptidomimetic science
  • Organic chemistry
  • Polymer science

Background:

  • Peptidomimetic oligomers like beta-peptides and peptoids (N-alkylglycine oligomers) are well-established.
  • Research is expanding to include hybrid structures with mixed backbones.

Purpose of the Study:

  • To survey the literature on hybrid structures of alpha-amino acids and peptoids.
  • To provide an overview of alpha/beta-peptides and beta-peptoids.

Main Methods:

  • Literature review
  • Survey of existing research

Main Results:

  • Identified hybrid structures of alpha-amino acids and peptoids as an emerging research area.
  • Highlighted the investigation of alpha/beta-peptides and beta-peptoids.

Conclusions:

  • Hybrid peptidomimetics, including alpha/beta-peptides and peptoids, represent a growing field.
  • Further research in this area is warranted to explore their potential.