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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
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Protein Folding

Protein Folding

Protein Organization

Protein Organization

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 Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein and Protein Structure

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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.
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Related Experiment Video

Updated: May 28, 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

Alpha-helical peptide assemblies giving new function to designed structures.

Elizabeth H C Bromley¹, Kevin J Channon

¹Department of Physics, Durham University, Durham, United Kingdom.

Progress in Molecular Biology and Translational Science

|October 18, 2011

Summary

This summary is machine-generated.

Scientists are advancing the design of alpha-helical tectons for self-assembly. Research now focuses on creating complex structures and functionalized fibers, moving beyond basic coiled-coil topologies.

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Last Updated: May 28, 2026

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

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

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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

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Area of Science:

Biomolecular engineering
Supramolecular chemistry
Materials science

Background:

The design of alpha-helical tectons for self-assembly is a rapidly advancing scientific discipline.
Reliable production and validation of various coiled-coil topologies in synthetic systems have been achieved.

Purpose of the Study:

To discuss progress in the design of discrete alpha-helical tecton structures.
To review advancements in the design of infinite or fiber assemblies.
To outline future challenges in self-assembling tecton systems.

Main Methods:

Utilizing synthetic systems for the production and validation of coiled-coil topologies.
Developing modified and functionalized fibers through advanced design principles.

Main Results:

Demonstrated reliable production of diverse coiled-coil topologies.
Successfully created functionalized fibers with tailored properties.
Established a foundation for designing more complex, discrete self-assembling structures.

Conclusions:

The field of alpha-helical tecton design for self-assembly has matured significantly.
Current research is progressing towards complex structures and functionalized materials.
Further challenges remain in realizing advanced applications and intricate designs.