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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 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 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...

Protein Folding

Protein Folding

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 Organization

Protein Organization

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Related Experiment Video

Updated: May 31, 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

Self-assembly and dynamics of polypeptides.

George Floudas¹, Hans Wolfgang Spiess

¹Max-Planck-Institut für Polymerforschung, 55021 Mainz, Germany; Department of Physics, University of Ioannina, P.O. Box 1186, GR-45110 Ioannina, Greece and FORTH, Biomedical Research Institute (BRI), Greece. gfloudas@cc.uoi.gr.

Macromolecular Rapid Communications

|June 28, 2011

Summary

Polypeptide dynamics and self-assembly were studied using advanced techniques. Defected hydrogen bonds were found to cause the glass transition and reduce alpha-helix stability.

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Area of Science:

Biophysics
Polymer Science
Materials Science

Background:

Understanding polypeptide self-assembly is crucial for biomaterials.
The glass transition in polypeptides affects their material properties.
Secondary structures like alpha-helices are fundamental to polypeptide function.

Purpose of the Study:

To investigate the hierarchical self-assembly and dynamics of polypeptides.
To elucidate the origin of the glass transition in these systems.
To determine how topology and packing influence secondary structure persistence.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy
X-ray scattering
Dielectric spectroscopy

Main Results:

A network of defected hydrogen bonds was identified as the cause of dynamics freezing at the liquid-to-glass transition.
Defected hydrogen-bonded regions were shown to decrease the persistence length of alpha-helices.
Block copolypeptides offer a method to control secondary structure type and persistence.

Conclusions:

The study provides insights into the molecular origins of the glass transition in polypeptides.
Defected hydrogen bonds play a critical role in limiting secondary structure stability.
Engineered copolypeptides can be used to tailor polypeptide structural properties.