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 Experiment Videos

Flexibility and function in HIV-1 protease

L K Nicholson1, T Yamazaki, D A Torchia

  • 1Molecular Structural Biology Unit, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892, USA.

Nature Structural Biology
|April 1, 1995
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Mammary gland responses to supplementation of rumen-protected methionine products in dairy cows.

Journal of dairy science·2026
Same author

Nose-to-brain translocation of inhaled ultrafine elongated particles: facts and mysteries.

Frontiers in toxicology·2025
Same author

Emerging applications of gene editing technologies for the development of climate-resilient crops.

Frontiers in genome editing·2025
Same author

Heat stress-associated changes in the intestinal barrier, inflammatory signals, and microbiome communities in dairy calves.

Journal of dairy science·2023
Same author

A robust experimental and computational analysis framework at multiple resolutions, modalities and coverages.

Frontiers in immunology·2022
Same author

Drivers of avian habitat use and detection of backyard birds in the Pacific Northwest during COVID-19 pandemic lockdowns.

Scientific reports·2022
Same journal

Fingering nucleic acids: the RNA did it.

Nature structural biology·2003
Same journal

Histone H1.2 as a trigger for apoptosis.

Nature structural biology·2003
Same journal

Tom40: more than just a channel.

Nature structural biology·2003
Same journal

Announcing the worldwide Protein Data Bank.

Nature structural biology·2003
Same journal

Small RNAs come of age.

Nature structural biology·2003
Same journal

Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.

Nature structural biology·2003
See all related articles

HIV protease dynamics were studied using NMR. Flexible flaps on the HIV protease (human immunodeficiency virus protease) are crucial for enzyme function, allowing substrate entry and product release.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Virology

Background:

  • HIV protease is essential for viral replication.
  • Understanding HIV protease dynamics is key to developing effective inhibitors.

Purpose of the Study:

  • To investigate the molecular dynamics of HIV protease bound to high-affinity inhibitors.
  • To elucidate the role of protein backbone motions in enzyme function.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Analysis of 15N spin relaxation parameters.

Main Results:

  • Significant internal motions of the HIV protease backbone were detected.
  • Flap terminal loops exhibit large-amplitude motions (ps-ns timescale).

Related Experiment Videos

  • Flap tips undergo conformational exchange (microsecond timescale).

    • Conclusions:

    • HIV protease flap flexibility is essential for its function.
    • Flexible flaps facilitate substrate access and product release from the active site.