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Protein Organization

Protein Organization

Protein Folding

Protein Folding

Peptide Bonds

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 Structure

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...

Protein Organization

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 Folding

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...

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Related Experiment Video

Updated: Jun 9, 2026

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

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

Published on: November 21, 2013

Double helix formation in alpha-peptides: a theoretical study.

Peter Schramm¹, Hans-Jörg Hofmann

¹Institute of Biochemistry, Pharmacy, and Psychology, University of Leipzig, Leipzig, Germany.

Journal of Peptide Science : an Official Publication of the European Peptide Society

|May 18, 2010

Summary

This study explores hydrogen bonding in peptide double helices using advanced computational methods. Antiparallel helices composed of alternating L- and D-amino acids are found to be the most stable structures.

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Area of Science:

Computational chemistry
Molecular biophysics
Peptide science

Background:

Understanding peptide secondary structures is crucial for molecular biology.
Hydrogen bonding dictates the stability and formation of peptide helices.

Purpose of the Study:

To provide a comprehensive analysis of hydrogen bonding patterns in alpha-peptide double helices.
To investigate the influence of strand orientation and amino acid composition on helix stability.

Main Methods:

Ab initio molecular orbital theory was employed for theoretical calculations.
Analysis covered both antiparallel and parallel double helix configurations.

Main Results:

Antiparallel double helices exhibit superior stability compared to parallel ones.
Stable double helices require alternating L- and D-amino acids in peptide strands.
Stability was benchmarked against competing single-stranded helices.

Conclusions:

The findings elucidate secondary structure formation in peptides.
This research provides a foundation for designing novel membrane channels with specific peptide sequences.