Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Size and Structure of Viral Genomes

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...

You might also read

Related Articles

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

Sort by

Same author

Mutations in the WFYY motif alter human PrimPol activity: structural insights from atomistic MD simulations.

Physical chemistry chemical physics : PCCP·2026

Same author

A geometric criterion links HIV-1 capsid topography to its biophysical properties and function.

Nature communications·2026

Same author

A geometric criterion links HIV-1 capsid topography to its biophysical properties and function.

bioRxiv : the preprint server for biology·2026

Same author

Lenacapavir prevents production of infectious HIV-1 by abrogating immature virus assembly.

bioRxiv : the preprint server for biology·2026

Same author

Stoichiometric binding of Cyclophilin-A to the HIV-1 capsid modulates its mechanoelastic properties.

bioRxiv : the preprint server for biology·2026

Same author

Integrase anchors viral RNA to the HIV-1 capsid interior.

Nature·2026

Same journal

Predicting Nirmatrelvir Resistance in SARS-CoV-2 M<sup>pro</sup> Mutants with an Integrated Computational Framework.

The journal of physical chemistry. B·2026

Same journal

From Cation Solvation to Anion Coordination: Lewis-Acidic Boranes Enable Halide Salt Electrolytes.

The journal of physical chemistry. B·2026

Same journal

In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.

The journal of physical chemistry. B·2026

Same journal

Metastructure Analysis of Self-Assembled Nanocubes with Different Equatorial Methyl Groups Based on Molecular Dynamics Simulations.

The journal of physical chemistry. B·2026

Same journal

A Cocoordinated <sup>1</sup>H Internal Reference Quantifies Proton-Exchange Bias in Coordinated-Water Diffusion.

The journal of physical chemistry. B·2026

Same journal

Unveiling Electrolyte-Dependent Coordination Site Dynamics for Redox Mediator Design in Lithium-O<sub>2</sub> Batteries: Exchange vs Rearrangement.

The journal of physical chemistry. B·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jan 8, 2026

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1 T = 4 Capsids.

Amanda C Macke¹, Chaoyi Xu¹, Sruthi Sudhakar¹

¹Department of Chemistry & Biochemistry, University of Delaware, Newark, Delaware 19716, United States.

The Journal of Physical Chemistry. B

|December 22, 2025

Summary

This summary is machine-generated.

Inositol hexakisphosphate (IP6) stabilizes the HIV-1 capsid. Molecular simulations show IP6 binding is hindered by capsid structure, but its presence minimally impacts overall capsid dynamics or ion flow.

More Related Videos

In vitro Uncoating of HIV-1 Cores

In vitro Uncoating of HIV-1 Cores

Published on: November 8, 2011

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Published on: November 4, 2018

Related Experiment Videos

Last Updated: Jan 8, 2026

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers

Published on: March 8, 2012

In vitro Uncoating of HIV-1 Cores

In vitro Uncoating of HIV-1 Cores

Published on: November 8, 2011

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Published on: November 4, 2018

Area of Science:

Structural biology
Virology
Computational biophysics

Background:

The HIV-1 capsid's structure is crucial for its function.
Inositol hexakisphosphate (IP6) is known to interact with the HIV-1 capsid.

Purpose of the Study:

To investigate the relationship between IP6, capsid architecture, and the environment.
To understand how local molecular interactions influence global capsid behavior.

Main Methods:

Utilized in silico molecular dynamics simulations.
Performed simulations on T = 4 icosahedral capsids with and without IP6, and with the R18L mutation.
Employed unbiased flooding simulations to study IP6 translocation.

Main Results:

IP6 binding is thermodynamically favorable in pentamers but faces kinetic barriers at hexameric pores.
The R18 ring and β-hairpins impede spontaneous IP6 translocation.
Local IP6 binding events and the R18L mutation had minimal effect on global capsid dynamics or ion flux.

Conclusions:

IP6 acts as a dynamic stabilizer for the HIV-1 capsid.
Capsid morphology primarily governs functional properties like dynamics and ion flux.
Capsid geometry plays a key role in modulating structural and functional behavior.