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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.
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...
What are Viruses?00:50

What are Viruses?

Overview
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

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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

Nucleocapsid structure and function.

S Longhi1

  • 1Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Universités Aix-Marseille I et II, 163 avenue de Luminy, Case 932, 13288 Marseille Cedex 09, France. Sonia.Longhi@afmb.univ-mrs.fr

Current Topics in Microbiology and Immunology
|February 10, 2009
PubMed
Summary
This summary is machine-generated.

Measles virus nucleoprotein (N) has a structured core and a disordered tail. This tail

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Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
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Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

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

Related Experiment Videos

Last Updated: Jun 25, 2026

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

Published on: July 27, 2021

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis (NAME) Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

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

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Measles virus (MeV) is a Paramyxoviridae family member.
  • Its genome is a single-stranded, negative-sense RNA.
  • The nucleoprotein (N) encapsidates the genome, forming a ribonucleoprotein complex essential for transcription and replication.

Purpose of the Study:

  • To describe the structural information of the MeV nucleoprotein (N).
  • To propose models for MeV transcription and replication mechanisms.
  • To discuss the functional implications of structural disorder in MeV proteins.

Main Methods:

  • Structural analysis of the nucleoprotein.
  • Modeling of protein-RNA interactions.
  • Analysis of intrinsically disordered protein regions.

Main Results:

  • The MeV nucleoprotein consists of a structured core (N(CORE)) and a disordered C-terminal domain (N(TAIL)).
  • A model is proposed where N(TAIL) dynamics facilitate polymerase complex (L-P) movement on the nucleocapsid template.
  • Flexibility in disordered N and P domains enables tripartite complex formation (No-P-L) during replication.

Conclusions:

  • The structural disorder of MeV nucleoprotein and phosphoprotein plays a crucial role in viral replication.
  • Disordered regions facilitate dynamic interactions with multiple partners, leading to diverse biological effects.
  • Understanding these mechanisms can inform antiviral strategies.