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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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...
DNA Helicases00:55

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
Viruses with RNA Genomes01:29

Viruses with RNA Genomes

RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
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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.
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Size and Structure of Viral Genomes

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Related Experiment Video

Updated: Jun 18, 2026

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

HIV-1 nucleocapsid protein bends double-stranded nucleic acids.

Hui Wang1, Yu-Shan Yeh, Paul F Barbara

  • 1Center for Nano and Molecular Science and Technology and Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas 78712, USA.

Journal of the American Chemical Society
|November 19, 2009
PubMed
Summary

The human immunodeficiency virus type-1 nucleocapsid protein induces sharp bending in double-stranded DNA and DNA/RNA. This newly discovered interaction may play a role in viral DNA condensation during the HIV-1 life cycle.

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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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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

Related Experiment Videos

Last Updated: Jun 18, 2026

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

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

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:

  • Molecular Biology
  • Virology
  • Biophysics

Background:

  • The HIV-1 nucleocapsid (NC) protein is multifunctional and binds nucleic acids (NAs) non-specifically.
  • NC's known function involves partially melting structured NAs, facilitating HIV-1 reverse transcription.
  • This function is attributed to NC's preference for single-stranded bases.

Purpose of the Study:

  • To investigate a previously undiscovered mode of interaction between NC protein and nucleic acids.
  • To probe NC-induced bending of fully duplexed DNA/DNA and DNA/RNA segments.
  • To analyze associated heterogeneous conformational dynamics in model NC/NA complexes.

Main Methods:

  • Single-molecule fluorescence resonance energy transfer (SM-FRET) in vitro.
  • Utilizing model NC/NA complexes to study interactions.
  • Analyzing conformational dynamics of nucleic acid segments.

Main Results:

  • A novel mode of NC/NA interaction was identified: NC-induced sharp bending of duplex DNA/DNA and DNA/RNA.
  • Heterogeneous conformational dynamics associated with NC-induced bending were observed.
  • NC demonstrates an ability to bend fully double-stranded nucleic acid segments.

Conclusions:

  • NC protein can induce significant bending in duplex nucleic acids, a previously unknown interaction.
  • This NC-induced NA bending may be biologically relevant for NC-mediated condensation of duplex proviral DNA.
  • The findings expand our understanding of NC's multifunctional role in the HIV-1 life cycle.