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Related Concept Videos

Viral Structure00:56

Viral Structure

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.
Protein Complex Assembly02:41

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 Complex Assembly02:41

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...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...
Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

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: Jun 25, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

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

Published on: July 27, 2021

Invariant polymorphism in virus capsid assembly.

Hung D Nguyen1, Vijay S Reddy, Charles L Brooks

  • 1Department of Chemistry and Biophysics Program, 930 North University Avenue, University of Michigan, Ann Arbor, Michigan 48109, USA.

Journal of the American Chemical Society
|February 10, 2009
PubMed
Summary
This summary is machine-generated.

Molecular simulations reveal conditions for viral capsid self-assembly. This study elucidates how temperature and protein concentration influence the formation of icosahedral capsids and aberrant structures, offering insights for controlled assembly.

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Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
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Published on: August 9, 2011

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
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In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

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Last Updated: Jun 25, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

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

Published on: July 27, 2021

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
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Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

Published on: August 9, 2011

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

Area of Science:

  • Biophysics
  • Materials Science
  • Computational Biology

Background:

  • Viral capsid self-assembly is crucial for materials science and medicine.
  • Understanding assembly mechanisms is limited by experimental challenges.

Purpose of the Study:

  • To elucidate viral protein self-assembly into icosahedral capsids using molecular simulations.
  • To identify conditions governing capsid formation and polymorphism.

Main Methods:

  • Geometrically realistic coarse-grained models.
  • Specialized molecular dynamics methods.
  • Simulation of coat protein concentration and temperature effects.

Main Results:

  • Spontaneous self-assembly of T = 1 and T = 3 icosahedral capsids observed.
  • Ubiquitous formation of nonicosahedral aberrant capsules alongside icosahedral products.
  • Structural polymorphism is an inherent property arising from condition-dependent kinetics.

Conclusions:

  • Insights into complex viral capsid assembly processes.
  • Identification of kinetic mechanisms for both icosahedral and aberrant capsule formation.
  • Potential for controlling capsid assembly by manipulating temperature and protein concentration.