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Protein Complex Assembly02:41

Protein Complex Assembly

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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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Viral Structure00:56

Viral Structure

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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...
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Subviral Agents01:29

Subviral Agents

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Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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Globular Proteins01:27

Globular Proteins

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In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
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Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

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Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
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Related Experiment Video

Updated: Jul 26, 2025

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

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Structural polymorphism in protein cages and virus-like particles.

Felicia Lie1, Taylor N Szyszka1, Yu Heng Lau1

  • 1School of Chemistry, The University of Sydney, Eastern Avenue, Sydney, NSW 2006, Australia. yuheng.lau@sydney.edu.au.

Journal of Materials Chemistry. B
|June 22, 2023
PubMed
Summary
This summary is machine-generated.

Protein cages and virus-like particles can form diverse shapes beyond uniform structures. Minor changes in conditions or protein sequences allow for varied architectures, crucial for biotechnology applications.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biotechnology

Background:

  • Protein cages and virus-like particles (VLPs) are typically viewed as highly uniform self-assembled structures.
  • Their assembly is often considered to follow strict geometric principles.
  • However, emerging evidence suggests greater structural flexibility than previously assumed.

Purpose of the Study:

  • To highlight the underappreciated diversity of architectures in protein cages and VLPs.
  • To categorize the polymorphic architectures based on their formation methods.
  • To emphasize the importance of structural diversity for biotechnological applications.

Main Methods:

  • Review of existing literature on protein cage and VLP self-assembly.
  • Categorization of polymorphic structures based on experimental conditions and protein sequence modifications.
  • Analysis of how different architectures impact protein cage function.

Main Results:

  • Identified numerous examples where protein cages and VLPs exhibit polymorphic behavior.
  • Demonstrated that minor alterations in experimental conditions or protein sequences can lead to different architectures from the same system.
  • Highlighted the link between specific architectures and their functional properties.

Conclusions:

  • The inherent polymorphism of protein cages and VLPs offers significant opportunities for bioengineering.
  • Understanding and controlling polymorphic assembly is key to tailoring these structures for advanced biotechnological applications.
  • Further research into the factors governing polymorphic formation will expand their utility.