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Protein Organization

Protein Organization

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 Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: Jun 10, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

Rational Crystal Contact Engineering for Programmable Self-Assembled Protein Architectures.

Mantas Liutkus¹, Adriana L Rojas², Aitziber L Cortajarena^1,3

¹Centre for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance, Paseo de Miramón 194, San Sebastian, 20014, Spain.

Angewandte Chemie (International Ed. in English)

|October 13, 2025

Summary

This summary is machine-generated.

Crystal contact engineering allows rapid design of diverse protein assemblies. This method reengineers 3D protein crystals into lower-dimension structures like nanotubes and ribbons for materials science.

Keywords:

CTPR protein Crystal engineering Electron microscopy Nanoengineering Self‐assembly

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Last Updated: Jun 10, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

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Published on: January 6, 2017

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

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Derivatization of Protein Crystals with I3C using Random Microseed Matrix Screening

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Published on: January 16, 2021

Area of Science:

Materials Science
Biotechnology
Supramolecular Chemistry

Background:

Designing ordered protein-based assemblies for materials science is complex.
Existing methods require significant time and effort.

Purpose of the Study:

To develop a rapid and rational approach for designing diverse protein assemblies.
To explore crystal lattice contact modulation for creating ordered supramolecular structures.

Main Methods:

Modulating crystal lattice contacts to control assembly dimensions.
Targeted disruption of crystal contacts and directional growth pre-biasing.
Reengineering 3D crystal lattices of tetratricopeptide repeat proteins.

Main Results:

Successfully constructed 2D crystals, 1D fibers, ribbons, and nanotubes.
Demonstrated the ability to restrict crystal growth in selected directions.
Achieved lower-dimension assemblies retaining parent crystal structural features.

Conclusions:

Crystal contact engineering offers a rapid and attractive strategy for designing ordered supramolecular protein assemblies.
The approach enables the creation of structurally diverse protein-based materials.
Leveraging existing crystal structures provides numerous engineering targets.