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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...

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Patterning of Microorganisms and Microparticles through Sequential Capillarity-assisted Assembly

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Design of a Hierarchical Assembly at a Solid-Liquid Interface Using an Asymmetric Protein Needle.

Kosuke Kikuchi¹, Koki Date¹, Takafumi Ueno^1,2

¹School of Life Science and Technology, Tokyo Institute of Technology, 4259-B-55, Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.

Langmuir : the ACS Journal of Surfaces and Colloids

|February 3, 2023

Summary

Researchers engineered hierarchical protein assemblies using anisotropic gene product 5 (gp5) protein needles. This novel approach bypasses symmetry constraints, enabling complex structures through distinct interaction sites.

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Last Updated: Aug 11, 2025

Patterning of Microorganisms and Microparticles through Sequential Capillarity-assisted Assembly

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Published on: November 4, 2021

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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

Area of Science:

Protein engineering
Biophysics
Materials science

Background:

Hierarchical protein assembly design is complex, requiring atomic precision.
Symmetry-based strategies limit resulting protein assembly structures.

Purpose of the Study:

To construct a hierarchical protein assembly using anisotropic protein needles.
To explore novel protein-protein interaction strategies beyond symmetry.

Main Methods:

Utilized anisotropic gene product 5 (gp5) protein from bacteriophage T4 with a C-terminal hexahistidine-tag (His-tag).
Employed high-speed atomic force microscopy (HS-AFM) for real-time surface imaging and analysis.

Main Results:

gp5_CHis formed tetrameric clusters via its N-terminal head on mica.
These clusters self-assembled into a network-like monolayer via the C-terminal His-tag.
HS-AFM confirmed a non-crystalline, network structure.

Conclusions:

Structural anisotropy provides a new paradigm for hierarchical protein assembly.
This method expands the available tools for designing complex protein structures.