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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
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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: May 27, 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

Supramolecular double helix from capped γ-peptide.

Suman Kumar Maity1, Sibaprasad Maity, Poulami Jana

  • 1Department of Chemical Sciences, Indian Institute of Science Education and Research Kolkata, Mohanpur, West Bengal 741252, India.

Chemical Communications (Cambridge, England)
|December 2, 2011
PubMed
Summary

Capped gamma-peptides form helical structures that self-assemble into double helices in the solid state. This self-assembly is driven by hydrogen bonding and pi-pi stacking interactions.

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Published on: August 1, 2018

Area of Science:

  • Supramolecular Chemistry
  • Peptide Chemistry
  • Crystallography

Background:

  • Gamma-peptides are non-natural amino acid analogues with potential applications in medicinal chemistry.
  • Understanding the self-assembly behavior of peptides is crucial for designing novel biomaterials and drug delivery systems.

Purpose of the Study:

  • To investigate the solid-state structure and self-assembly of capped gamma-peptides.
  • To elucidate the driving forces behind the formation of supramolecular structures in capped gamma-peptides.

Main Methods:

  • Single crystal X-ray diffraction was employed to determine the molecular and crystal structure.
  • Analysis of intermolecular interactions, including hydrogen bonding and pi-pi stacking, was performed.

Main Results:

  • The capped gamma-peptide was found to adopt a helical conformation in the solid state.
  • These helical peptides self-assemble into a parallel double helical supramolecular structure.
  • Intermolecular hydrogen bonding and pi-pi stacking interactions were identified as key stabilizing forces.

Conclusions:

  • Capped gamma-peptides can form stable helical structures that further assemble into double helical architectures.
  • Hydrogen bonding and pi-pi stacking are critical for the observed supramolecular organization.
  • The findings provide insights into the rational design of self-assembling peptide-based materials.