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Related Concept Videos

Urea Cycle01:23

Urea Cycle

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The urea cycle describes how liver cells convert ammonia to urea. Ammonia is a toxic waste product of protein catabolism. Land animals must convert ammonia into the less toxic urea which can be safely eliminated by the kidneys through urine. Marine animals excrete ammonia directly, and the surrounding water dilutes the ammonia to safe levels.
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Protein Folding01:22

Protein Folding

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Overview
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Protein Folding01:25

Protein Folding

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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.
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Preparation of 1° Amines: Hofmann and Curtius Rearrangement Overview01:07

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In the presence of an aqueous base and a halogen, primary amides can lose the carbonyl (as carbon dioxide) and undergo rearrangement to form primary amines. This reaction, called the Hofmann rearrangement, can produce primary amines (aryl and alkyl) in high yields without contamination by secondary and tertiary amines.
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The Hofmann and Curtius rearrangement reactions can be applied to synthesize primary amines from carboxylic acid derivatives such as amides and acyl azides. In the Hofmann rearrangement, a primary amide undergoes deprotonation in the presence of a base, followed by halogenation to generate an N-haloamide. A second proton abstraction produces a stabilized anionic species, which rearranges to an isocyanate intermediate via an alkyl group migration from the carbonyl carbon to the neighboring...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Updated: Oct 26, 2025

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Urea based foldamers.

Sung Hyun Yoo1, Bo Li1, Christel Dolain1

  • 1University of Bordeaux, CNRS, Bordeaux INP, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, Pessac, France.

Methods in Enzymology
|July 30, 2021
PubMed
Summary

N,N'-linked oligoureas are amino acid-free peptidomimetics that form predictable helical structures. Protocols are provided for synthesizing these oligoureas and peptide-oligourea hybrids for diverse applications.

Keywords:
Chimeric peptide/oligourea helicesFoldamersHelixOligoureaPeptide mimicryProtein-protein interactionsProtein-surface recognitionSolid-phase synthesis

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Area of Science:

  • Organic Chemistry
  • Polymer Chemistry
  • Medicinal Chemistry

Background:

  • N,N -linked oligoureas are sequence-defined peptidomimetics.
  • They mimic peptide alpha-helices, offering predictable helical structures.
  • Oligoureas possess synthetic accessibility, sequence modularity, and folding fidelity.

Purpose of the Study:

  • To provide detailed protocols for monomer preparation.
  • To outline the synthesis and purification of homo-oligoureas.
  • To describe the creation of peptide-oligourea hybrids.

Main Methods:

  • Monomer synthesis and purification.
  • Solid-phase or solution-phase oligomerization techniques.
  • Characterization of oligourea and hybrid structures.

Main Results:

  • Established protocols for synthesizing enantiopure N,N -linked oligoureas.
  • Demonstrated the formation of well-defined helical structures.
  • Successfully generated peptide-oligourea hybrids with enhanced properties.

Conclusions:

  • N,N -linked oligoureas are versatile foldamers with significant potential.
  • The developed protocols facilitate the synthesis of these molecules and hybrids.
  • Applications span medicinal chemistry, catalysis, and biomaterials.