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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

Protein Folding

Protein Folding

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-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Related Experiment Video

Updated: Mar 15, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Designing Covalently Linked Heterodimeric Four-Helix Bundles.

M Chino¹, L Leone¹, O Maglio²

¹University of Napoli Federico II, Napoli, Italy.

Methods in Enzymology

|September 3, 2016

Summary

This summary is machine-generated.

De novo protein design advances helical bundle creation. A new method enables covalent heterodimerization of alpha-helical proteins, creating asymmetric four-helix bundles for tailored functions.

Keywords:

Covalent linkage Cu(I) catalyzed azide–alkyne cycloaddition De novo design Diiron-oxo proteins Four-helix bundles Heterodimers Metalloprotein models

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

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Last Updated: Mar 15, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Area of Science:

Protein engineering
Biophysical chemistry
Synthetic biology

Background:

De novo protein design is crucial for understanding protein folding and function.
Four-helix bundles are common in nature, exemplified by diiron proteins involved in diverse biological processes.
Previous de novo designs focused on simpler helical bundles, with less emphasis on precise control over complex functions.

Purpose of the Study:

To develop a method for constructing asymmetric four-helix bundles via covalent heterodimerization.
To create minimal models of natural diiron proteins with reprogrammed functions.
To investigate how amino acid sequence and metal environments modulate protein function and selectivity.

Main Methods:

Utilized de novo design principles to create alpha-helical harpins.
Employed copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) for covalent linkage of two distinct helical monomers.
Developed a generalized protocol for creating variable linkers at different positions within the protein structure.

Main Results:

Successfully demonstrated the covalent heterodimerization of two different alpha-helical harpins to form asymmetric four-helix bundles.
Established a fast, cost-effective, and versatile method for protein-protein conjugation.
The method is adaptable for linking various peptide and protein combinations.

Conclusions:

The developed method provides a powerful tool for constructing bespoke asymmetric protein architectures.
This approach facilitates the creation of novel protein functions and the study of enzyme mechanisms.
The technique holds potential for applications in protein engineering, drug delivery, and biomaterials.