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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
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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Related Experiment Video

Updated: May 20, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

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

Published on: August 20, 2018

Covalent cross-linking within supramolecular peptide structures.

George W Preston1, Sheena E Radford, Alison E Ashcroft

  • 1School of Chemistry, Faculty of Biological Sciences, University of Leeds, Woodhouse Lane, Leeds LS2 9JT, UK.

Analytical Chemistry
|July 4, 2012
PubMed
Summary

This study uses a novel cross-linking method to map the structure of peptide nanostructures. The technique reveals how molecular arrangement influences cross-linking sites, offering insights into amyloid fibril formation.

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Related Experiment Videos

Last Updated: May 20, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

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

Published on: August 20, 2018

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

  • Biophysical Chemistry
  • Materials Science
  • Structural Biology

Background:

  • β-Sheet peptide nanostructures, like amyloid fibrils, are biologically significant and functionally relevant materials.
  • Determining the atomic resolution structure of these complex nanostructures is challenging.
  • Covalent cross-linking coupled with mass spectrometry offers a promising approach for structural analysis of small samples.

Purpose of the Study:

  • To investigate the cross-linking chemistry within morphologically distinct supramolecular structures of diazirine-functionalized peptides.
  • To explore the relationship between cross-linker properties, covalent cross-links, and noncovalent structure.
  • To demonstrate the utility of this cross-linking approach for obtaining structural restraints in ordered supramolecular assemblies.

Main Methods:

  • Utilized a pH-switchable system (Aβ(16-22)) incorporating a photoreactive diazirine-containing amino acid.
  • Employed ion mobility spectrometry coupled to mass spectrometry for separation and analysis of cross-linked products.
  • Applied chemical derivatization and tandem mass spectrometry to identify covalent cross-links.

Main Results:

  • Observed differences in cross-linking sites that are attributable to supramolecular templating effects.
  • Established a link between cross-linker chemistry, identified covalent cross-links, and the underlying noncovalent structure.
  • Validated the use of diazirine-based cross-linking for probing the architecture of peptide nanostructures.

Conclusions:

  • The diazirine-based cross-linking method provides valuable structural restraints for ordered supramolecular assemblies.
  • Supramolecular organization significantly influences the site-specific covalent cross-linking within peptide nanostructures.
  • Careful evaluation of cross-linked products is crucial for accurate structural interpretation.