Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

17.9K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.9K
Introduction to Virus01:28

Introduction to Virus

95
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...
95
Viral Structure00:56

Viral Structure

62.7K
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.
62.7K
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

67
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...
67
Subviral Agents01:29

Subviral Agents

48
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...
48
Protein Complex Assembly02:41

Protein Complex Assembly

10.7K
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...
10.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Quantifying species-specific binding affinities of transthyretin aggregation inhibitors.

Biophysical reports·2026
Same author

Linker Length and Composition within Disordered Binding Motifs Modulates the Avidity and Reversibility of a Multivalent Protein Interaction Switch.

Journal of molecular biology·2025
Same author

Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides.

The Journal of biological chemistry·2025
Same author

Linker Length and Composition within Disordered Binding Motifs modulates the Avidity and Reversibility of a Multivalent Protein Interaction Switch.

bioRxiv : the preprint server for biology·2025
Same author

Initiation of transthyretin aggregation at neutral pH by fluid agitation.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Aggregation of Transthyretin by Fluid Agitation.

bioRxiv : the preprint server for biology·2024

Related Experiment Video

Updated: Jul 26, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.0K

Vital for Viruses: Intrinsically Disordered Proteins.

H Jane Dyson1

  • 1Department of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Journal of Molecular Biology
|June 17, 2023
PubMed
Summary

Viruses utilize intrinsically disordered proteins (IDPs) as a versatile molecular toolkit for infection, assembly, and proliferation. These adaptable proteins are found across diverse viruses, highlighting their crucial role in viral life cycles.

Keywords:
Protein disorderpost-translational modificationprotein–protein interactionviral oncoproteinsvirus proteins

More Related Videos

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

26.0K
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

9.0K

Related Experiment Videos

Last Updated: Jul 26, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

2.0K
Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

26.0K
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

9.0K

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Viruses infect all life forms, exhibiting diverse genomes (DNA/RNA) and structures.
  • Intrinsically disordered proteins (IDPs) lack stable 3D structures but perform vital functions.
  • IDPs are prevalent across studied viruses, regardless of genome type or capsid structure.

Purpose of the Study:

  • To survey the diverse functions of intrinsically disordered proteins (IDPs) in viruses.
  • To illustrate the wide-ranging roles of IDPs in viral infection, assembly, and proliferation.
  • To highlight the expanding field of viral IDP research.

Main Methods:

  • Review of existing scientific literature on viral intrinsically disordered proteins.
  • Compilation of case studies showcasing IDP functions in various viral systems.
  • Synthesis of information on the prevalence and roles of IDPs in virology.

Main Results:

  • Intrinsically disordered proteins are a common feature in viruses.
  • IDPs contribute to essential viral processes such as infection, replication, and assembly.
  • The functions of viral IDPs are diverse and adaptable to different viral strategies.

Conclusions:

  • Intrinsically disordered proteins represent a key molecular toolkit for viruses.
  • The study of viral IDPs is a rapidly growing and important area of research.
  • Understanding IDP functions provides insights into viral mechanisms and potential therapeutic targets.