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

Kinetically robust monomeric protein from a hyperthermophile.

Atsushi Mukaiyama1, Kazufumi Takano, Mitsuru Haruki

  • 1Department of Material and Life Science, Osaka University, Yamadaoka, Suita 565-0871, Japan.

Biochemistry
|October 27, 2004
PubMed
Summary

This study reveals that the hyperthermophilic protein Tk-RNase HII achieves high stability through remarkably slow unfolding kinetics, maintaining reversible two-state folding. These findings offer insights into protein stabilization mechanisms in extreme environments.

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

Data sets on the interaction of FKBP35 from <i>Plasmodium knowlesi</i> and Hsp90 C-terminal pentapeptide.

Data in brief·2026
Same author

Diversity and Plant Growth-Promoting Potential of Duckweed-Associated Bacteria on Wolffia globosa Biomass Production and Nutritional Quality.

Environmental microbiology reports·2026
Same author

Dual functions of nonionic surfactant Tween-20 in enhancing productivity and elution efficiency of alkylresorcinols from Azotobacter vinelandii.

Biotechnology letters·2026
Same author

Standardized Ileal Digestibility of Protein and Amino Acids in Black Soldier Fly Larvae and Duckweed in Broiler Chickens.

Animals : an open access journal from MDPI·2026
Same author

Species-level profiling of <i>Landoltia punctata</i> (duckweed) microbiome under nutrient stress using full-length 16S rRNA sequencing.

PeerJ·2026
Same author

Complete genome sequence of a member of a potentially novel genus within the family Opitutaceae isolated from a liquid medium used for co-cultivating duckweeds and river water-derived microbes.

Microbiology resource announcements·2025

Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Folding and Stability
  • Extremophile Biology

Background:

  • Hyperthermophilic proteins exhibit remarkable stability, crucial for survival in extreme environments.
  • Understanding the energetic features of protein folding is key to elucidating stability mechanisms.
  • Ribonuclease HII (RNase HII) from Thermococcus kodakaraensis (Tk-RNase HII) is a monomeric protein from a hyperthermophile.

Purpose of the Study:

  • To investigate the energetic features contributing to the high stability of Tk-RNase HII.
  • To clarify the equilibrium and kinetic aspects of Tk-RNase HII unfolding and refolding under denaturation conditions.
  • To compare the kinetic properties of Tk-RNase HII with homologous proteins from other organisms.

Main Methods:

Related Experiment Videos

  • Guanidine hydrochloride (GdnHCl)-induced unfolding and refolding monitored by circular dichroism (CD) at 220 nm.
  • Heat-induced denaturation analyzed using differential scanning calorimetry (DSC).
  • Kinetic studies to determine unfolding and refolding rate constants.

    • Main Results:

    • Both GdnHCl- and heat-induced denaturation of Tk-RNase HII are highly reversible and approximate a two-state model.
    • Unfolding of Tk-RNase HII is remarkably slow, requiring extended periods (2 weeks) to reach equilibrium at 50°C.
    • Unfolding rate constants for Tk-RNase HII are significantly lower than those of E. coli RNase HI and Thermus thermophilus RNase HI, while refolding rates are comparable.

    Conclusions:

    • The high stability of Tk-RNase HII is primarily attributed to its exceptionally slow unfolding rate.
    • The protein exhibits reversible two-state folding, a characteristic stabilization mechanism for this hyperthermophilic monomeric protein.
    • Kinetic data supports the thermodynamic equilibrium measurements, confirming the two-state folding model.