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Related Concept Videos

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.
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

Overview
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...

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Related Experiment Video

Updated: Jul 13, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Bend-ribbon forming gamma-peptides.

Abhishek Kothari1, M Khurram N Qureshi, Elizabeth M Beck

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW.

Chemical Communications (Cambridge, England)
|July 5, 2007
PubMed
Summary

Tetrameric gamma-peptide derivatives with constrained backbones adopt a bend-ribbon structure in solution. This conformation is stabilized by internal hydrogen bonds, offering insights into peptide folding.

Area of Science:

  • Organic Chemistry
  • Supramolecular Chemistry
  • Biophysical Chemistry

Background:

  • Gamma-peptide derivatives are peptidomimetics with potential applications in drug design.
  • Constraining peptide backbones can influence their secondary structures and biological activity.
  • Understanding the solution-state conformations of constrained peptides is crucial for predicting their interactions.

Purpose of the Study:

  • To investigate the solution conformation of homo- and heterochiral tetrameric gamma-peptide derivatives with backbone constraints.
  • To elucidate the role of intramolecular hydrogen bonds in stabilizing the observed conformation.
  • To explore the impact of chirality on the conformational preferences of these constrained peptides.

Main Methods:

  • Synthesis of homo- and heterochiral tetrameric gamma-peptide derivatives incorporating a five-membered ring constraint.

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Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides

Published on: January 12, 2009

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  • Solution-state conformational analysis using Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Computational modeling to support experimental findings and analyze hydrogen bonding networks.

    • Main Results:

    • Tetrameric gamma-peptide derivatives consistently adopted a bend-ribbon secondary structure in solution.
    • Intramolecular hydrogen bonds were identified as key stabilizing forces for the bend-ribbon conformation.
    • Both homo- and heterochiral derivatives populated this conformation, suggesting robustness to chirality.

    Conclusions:

    • Constrained tetrameric gamma-peptide derivatives exhibit a stable bend-ribbon conformation in solution.
    • The five-membered ring constraint effectively directs the peptide folding.
    • Intramolecular hydrogen bonding plays a critical role in the conformational stability of these novel peptide structures.