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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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Protein Complex Assembly

Protein Complex Assembly

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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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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Published on: November 21, 2013

Two-Dimensional Peptide and Protein Assemblies.

Elizabeth Magnotti¹, Vincent Conticello²

¹Department of Chemistry, Emory University, 1515 Dickey Drive, 30322, Atlanta, GA, USA.

Advances in Experimental Medicine and Biology

|September 29, 2016

Summary

This review explores two-dimensional peptide and protein nanosheets for precise molecular arrangement in nanoarchitectonics. Understanding these assemblies is key to designing functional nanoscale devices with controlled molecular structures.

Keywords:

Nanoarchitectonics Nanomaterials Nanosheets Peptide assemblies Protein assemblies Protein layers Protomers

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Area of Science:

Materials Science
Nanotechnology
Biochemistry

Background:

Two-dimensional nanoscale assemblies, or nanosheets, offer precise platforms for molecular and supramolecular arrangement.
Nanoarchitectonics, a strategy for fabricating nanoscale devices, has seen significant growth.
Sequence-specific biomolecules like peptides and proteins are ideal substrates for creating 2D nanoarchitectonics.

Purpose of the Study:

To review existing two-dimensional peptide and protein assemblies.
To advance the understanding of controlling molecular arrangement in two-dimensional systems.
To foster the development of rational design principles for peptide and protein nanosheets.

Main Methods:

Literature review of established two-dimensional peptide and protein assemblies.
Analysis of molecular-level instructions encoded within monomer sequences.
Exploration of design principles for controlling supramolecular structure.

Main Results:

Identified key characteristics of known 2D peptide and protein assemblies.
Highlighted the potential of biomolecular sequences for directing supramolecular organization.
Acknowledged the nascent stage of rational design principles due to protomer interaction complexity.

Conclusions:

Two-dimensional peptide and protein assemblies are crucial for advanced nanoarchitectonics.
Further research into design principles is needed to fully harness biomolecules for controlled 2D structures.
This review provides a foundation for future advancements in designing functional nanoscale devices.