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Related Concept Videos

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

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Protein Organization01:13

Protein Organization

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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 Organization01:24

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.

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Updated: May 28, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Self-assembled peptide architecture with a tooth shape: folding into shape.

Sunbum Kwon1, Hye Sun Shin, Jintaek Gong

  • 1Molecular-Level Interface Research Center, Department of Chemistry, KAIST, Daejeon 305-701, Korea.

Journal of the American Chemical Society
|October 12, 2011
PubMed
Summary

Researchers demonstrate controlled 3D molecular self-assembly using a helical β-peptide foldamer. This artificial protein fragment forms a unique molar tooth-shaped structure in aqueous solution, mimicking natural collagen architectures.

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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Molecular self-assembly is crucial for creating functional systems.
  • 2D self-assembly is well-studied, but 3D molecular self-assembly remains challenging.
  • Artificial protein fragments (foldamers) offer potential for controlled self-assembly.

Purpose of the Study:

  • To investigate the 3D self-assembly of a helical β-peptide foldamer.
  • To create novel 3D molecular architectures.
  • To understand the molecular arrangement in the self-assembled structure.

Main Methods:

  • Synthesis of a helical β-peptide foldamer with defined secondary structure.
  • Inducing self-assembly in aqueous solution.
  • Powder X-ray diffraction (PXRD) analysis.
  • Global optimization and Rietveld refinement for structural determination.

Main Results:

  • The β-peptide foldamer self-assembled into an unprecedented 3D molecular architecture.
  • The structure exhibited a distinct molar tooth shape.
  • PXRD and computational methods elucidated the molecular arrangement.
  • Four left-handed helical monomers formed a right-handed superhelix within the unit cell.

Conclusions:

  • Helical β-peptide foldamers can controllably form complex 3D molecular structures.
  • The self-assembled structure resembles the supercoiled architecture of collagen.
  • This work advances the field of 3D molecular self-assembly and biomimetic materials.