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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 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 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.
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...

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Related Experiment Video

Updated: Jun 3, 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

Structural transition in peptide nanotubes.

Nadav Amdursky1, Peter Beker, Itai Koren

  • 1Department of Molecular Microbiology and Biotechnology, George S Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.

Biomacromolecules
|March 11, 2011
PubMed
Summary
This summary is machine-generated.

Bioinspired peptide nanotubes undergo an irreversible conformational change, altering their nanocrystalline structure and significantly impacting properties from molecular to macroscopic levels.

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Area of Science:

  • Materials Science
  • Biomaterials Science
  • Nanotechnology

Background:

  • Phase transitions in materials are classically linked to changes in crystal space group symmetry, altering physical properties.
  • Peptide nanotubes (PNTs) are bioinspired nanomaterials with potential applications driven by their unique structures.

Purpose of the Study:

  • To investigate conformational induced transitions in peptide nanotubes (PNTs).
  • To characterize the resulting changes in nanocrystalline structure and material properties.

Main Methods:

  • Observation of molecular assembly changes from linear to cyclic peptide conformations.
  • Analysis of nanocrystalline structure transitions from hexagonal to orthorhombic space groups.
  • Evaluation of alterations in molecular, morphological, piezoelectric, second harmonic generation, and wettability properties.

Main Results:

  • Peptide nanotubes (PNTs) exhibit an irreversible conformational transition from linear to cyclic structures.
  • This transition induces a shift in nanocrystalline symmetry from noncentrosymmetric hexagonal to centrosymmetric orthorhombic.
  • Profound changes in PNT properties were observed at both microscopic and macroscopic scales.

Conclusions:

  • Conformational changes in PNTs can drive significant, irreversible phase transitions.
  • These transitions lead to substantial modifications in material properties, offering new avenues for material design.
  • The study highlights the potential of bioinspired peptide nanotubes in advanced material applications.