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Protein Complex Assembly

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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.
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Related Experiment Video

Updated: May 6, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

New designed protein assemblies.

Sabina Božič¹, Tibor Doles, Helena Gradišar

¹Department of Biotechnology, National Institute of Chemistry, Ljubljana, Slovenia.

Current Opinion in Chemical Biology

|November 5, 2013

Summary

This summary is machine-generated.

Scientists designed a novel polypeptide tetrahedron using a protein origami strategy. This approach arranges coiled-coil modules to create complex self-assembling protein nanostructures from a single chain.

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Last Updated: May 6, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Published on: July 17, 2019

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

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Published on: April 8, 2020

Area of Science:

Biochemistry
Structural Biology
Nanotechnology

Background:

Self-assembly is fundamental to biological systems, with polypeptides assembling into complex structures.
Designing novel protein folds remains a significant challenge in structural biology.
Previous methods focused on linking existing domains or engineering interfaces for protein assemblies.

Purpose of the Study:

To introduce a new strategy for designing self-assembling polypeptide folds.
To demonstrate the creation of a polypeptide tetrahedron using a protein origami approach.
To explore the use of topological arrangement of coiled-coil modules for nanostructure design.

Main Methods:

Utilizing a protein origami strategy based on the topological arrangement of coiled-coil modules.
Designing a single polypeptide chain by concatenating coiled-coil forming building modules.
Interspersing flexible hinges between modules to facilitate self-assembly.
Defining the final polypeptide nanostructure fold through the specific order of coiled-coil segments.

Main Results:

Successful design of a polypeptide tetrahedron nanostructure.
Demonstration of self-assembly driven by the topological arrangement of coiled-coil modules.
Validation of the protein origami strategy for creating de novo protein folds.

Conclusions:

The proposed protein origami strategy offers a novel route for designing self-assembling polypeptide nanostructures.
The order of coiled-coil segments is a critical determinant of the final fold in this design approach.
This method advances the field of protein design and nanotechnology by enabling the creation of complex, single-chain assemblies.