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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.
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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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Spindle Assembly

Spindle Assembly

Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Related Experiment Video

Updated: Feb 15, 2026

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

Engineering of protein assemblies within cells.

Tien K Nguyen¹, Takafumi Ueno¹

¹Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.

Current Opinion in Structural Biology

|January 10, 2018

Summary

This summary is machine-generated.

Researchers are engineering protein assemblies within cells, creating advanced biosupramolecular composites for biomaterials and biotechnology. This review highlights progress in cell-based fabrication and the exciting properties of these novel protein structures.

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Engineering Cell-permeable Protein

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Area of Science:

Biomaterials Science
Biotechnology
Synthetic Biology

Background:

Protein assemblies are crucial for cellular functions.
Recent advances enable the engineering of protein assemblies within living cells.
Biosupramolecular composites offer versatile applications.

Purpose of the Study:

To review recent advancements in engineering protein assemblies within cells.
To highlight the fabrication methods for intracellular protein assemblies.
To describe the promising properties and applications of these engineered assemblies.

Main Methods:

Review of literature on protein engineering and supramolecular assembly.
Analysis of biological and physicochemical approaches for in-cell fabrication.
Discussion of methods for creating complex protein structures within living systems.

Main Results:

Engineered protein assemblies can be efficiently fabricated within living cells.
These intracellular assemblies form novel biosupramolecular composites.
The properties of these composites are promising for various applications.

Conclusions:

Engineering protein assemblies within cells represents a significant advancement in biomaterials and biotechnology.
Intracellular fabrication offers new avenues for creating functional biosupramolecular materials.
Further research promises expanded applications in diverse fields.