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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...
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.

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Related Experiment Video

Updated: Jun 6, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
12:38

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

Published on: August 9, 2011

Modeling capsid self-assembly: design and analysis.

D C Rapaport1

  • 1Department of Physics, Bar-Ilan University, Ramat-Gan 52900, Israel. rapaport@mail.biu.ac.il

Physical Biology
|December 15, 2010
PubMed
Summary
This summary is machine-generated.

Simulations reveal that virus capsid self-assembly occurs through reversible stages, not irreversible ones. This cascade of events leads to efficient formation of stable viral structures.

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

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Related Experiment Videos

Last Updated: Jun 6, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
12:38

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

Published on: August 9, 2011

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
09:47

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Published on: March 1, 2012

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

Area of Science:

  • Biophysics
  • Computational Biology
  • Structural Biology

Background:

  • Virus capsid self-assembly is a fundamental biological process.
  • Understanding this process is key to virology and drug development.
  • Simplified models are valuable for studying complex biological systems.

Purpose of the Study:

  • To elucidate the self-assembly dynamics of spherical virus capsids using computational simulations.
  • To explore the influence of model parameters (e.g., size, reversibility, solvent) on assembly pathways.
  • To analyze growth pathways and intermediate states that are difficult to study experimentally.

Main Methods:

  • Utilized molecular dynamics simulations with simplified, low-resolution models.
  • Investigated polyhedral shells of varying sizes.
  • Incorporated both irreversible and reversible assembly pathways, with optional explicit solvent.
  • Developed and applied specific analysis techniques to study assembly dynamics.

Main Results:

  • Efficient viral capsid growth occurs via a cascade of highly reversible stages.
  • A vast number of potential partial assemblies exist, but only a few stable configurations are favored.
  • Simulation results provide insights into intermediate states and growth mechanisms.

Conclusions:

  • The self-assembly of virus capsids is predominantly driven by reversible interactions.
  • Simplified models effectively capture essential features of complex viral assembly.
  • Findings offer a deeper understanding of viral structure formation and potential therapeutic targets.