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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

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...

Assembly of Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

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Related Experiment Video

Updated: May 1, 2026

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

Hemoprotein-based supramolecular assembling systems.

Koji Oohora¹, Takashi Hayashi¹

¹Department of Applied Chemistry, Graduate School of Engineering, Osaka University Suita, 565-0871, Japan.

Current Opinion in Chemical Biology

|March 25, 2014

Summary

This review explores hemoprotein assemblies for biomaterials. Researchers are creating functional supramolecular structures from proteins like myoglobin and cytochromes.

Area of Science:

Biomaterials Science
Protein Engineering
Supramolecular Chemistry

Background:

Hemoproteins, metalloproteins containing iron porphyrin, are valuable for biomaterial development.
Rational design of hemoprotein assemblies is a key area of research.

Purpose of the Study:

To review recent advancements in the rational design of supramolecular hemoprotein assemblies.
To highlight the use of myoglobin, horseradish peroxidase, cytochrome b562, and cytochrome c as monomer units.

Main Methods:

Coordination bond-mediated assembly and domain swapping-mediated assembly for defined oligomers.
Hemoprotein reconstitution with synthetic heme derivatives for submicrometer structures (fibrils, vesicles/micelles, networks).

Main Results:

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

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

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Related Experiment Videos

Last Updated: May 1, 2026

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

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

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

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

Published on: February 6, 2020

Successfully created defined oligomers and various submicrometer-sized structures.
Demonstrated that assembled hemoprotein structures often retain their intrinsic functions.

Conclusions:

Chemical and biological strategies enable the creation of unique hemoprotein-based functional biomaterials.
These advancements pave the way for novel applications in biomaterials engineering.