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

Mitochondrial Precursor Proteins

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...

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...

Inhibitors of Virion Maturation and Assembly

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...

You might also read

Related Articles

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

Sort by

Same author

Type-1 inflammatory imprinting and programmed responsiveness to CD40L enhance Siglec-1-dependent HIV-1 trans-infection by dendritic cells.

Frontiers in immunology·2026

Same author

IL1RAP antibody-drug conjugates potently target primary and metastatic disease in multiple oncofusion-driven cancers.

Cancer discovery·2026

Same author

Senescence-related cytokine levels are associated with HIV-1 serostatus and persistence.

AIDS (London, England)·2025

Same author

Senescence-related cytokine levels are associated with HIV-1 serostatus and persistence.

medRxiv : the preprint server for health sciences·2025

Same author

Structural basis of deoxynucleotide addition by HIV-1 RT during reverse transcription.

Nature communications·2024

Same author

Antigen Presenting Cell-Mediated HIV-1 <i>Trans</i> Infection in the Establishment and Maintenance of the Viral Reservoir.

Medical research archives·2024

Search research articles

Related Experiment Video

Updated: Jun 4, 2026

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

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

Published on: January 19, 2015

Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution.

Tatiana V Ilina¹, Zhaoyong Xi¹, Teresa Brosenitsch¹

¹Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.

International Journal of Molecular Sciences

|December 18, 2020

Summary

Studying large proteins with Nuclear Magnetic Resonance (NMR) is difficult due to slow molecular tumbling. Using multiple NMR probes (like 1H, 19F, 13C, and 15N) helps overcome these challenges for structural and dynamic analysis.

Keywords:

HIV NMR isotope labeling protein reverse transcriptase ribonuclease H

More Related Videos

Determining 3'-Termini and Sequences of Nascent Single-Stranded Viral DNA Molecules during HIV-1 Reverse Transcription in Infected Cells

Determining 3'-Termini and Sequences of Nascent Single-Stranded Viral DNA Molecules during HIV-1 Reverse Transcription in Infected Cells

Published on: January 30, 2019

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

Related Experiment Videos

Last Updated: Jun 4, 2026

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

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

Published on: January 19, 2015

Determining 3'-Termini and Sequences of Nascent Single-Stranded Viral DNA Molecules during HIV-1 Reverse Transcription in Infected Cells

Determining 3'-Termini and Sequences of Nascent Single-Stranded Viral DNA Molecules during HIV-1 Reverse Transcription in Infected Cells

Published on: January 30, 2019

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

Area of Science:

Biophysics
Structural Biology
Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

Nuclear Magnetic Resonance (NMR) studies of large proteins (>100 kDa) in solution face significant technical challenges.
Increased molecular mass leads to slower tumbling, causing severe line-broadening and signal overlap in standard NMR spectra (e.g., 1H-13C, 1H-15N).
Selective isotope labeling strategies, while reducing signal complexity, can hinder comprehensive protein characterization.

Purpose of the Study:

To explore the utility of employing multiple NMR nuclei (1H, 19F, 13C, 15N) for characterizing large proteins.
To investigate the structural and dynamic properties of the 66 kDa homodimeric HIV-1 reverse transcriptase (p66/p66).
To understand the conformational changes during the maturation of the homodimer to the heterodimer (p66/p51) after HIV-1 protease cleavage.

Main Methods:

Utilized Nuclear Magnetic Resonance (NMR) spectroscopy with multiple isotope probes (1H, 19F, 13C, 15N).
Applied biophysical approaches to analyze protein structure and dynamics.
Complemented NMR data with biochemical assays.

Main Results:

Demonstrated that diverse NMR probes provide complementary information for large protein characterization.
Characterized the homodimeric state of HIV-1 reverse transcriptase (p66/p66).
Revealed conformational changes associated with the conversion to the heterodimeric form (p66/p51).

Conclusions:

The strategic use of multiple NMR nuclei is essential for overcoming technical limitations in studying large proteins.
This multi-probe NMR approach, combined with biochemical methods, provides comprehensive insights into protein structure, dynamics, and conformational transitions.
The study successfully elucidated aspects of HIV-1 reverse transcriptase homodimerization and its maturation process.