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

Characterizing the unstructured intermediates in oxidative folding.

Mahesh Narayan1, Ervin Welker, Harold A Scheraga

  • 1Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.

Biochemistry
|June 11, 2003
PubMed
Summary

A new method using trans-[Pt(en)(2)Cl(2)](2+) reveals that reduced RNase A has a bias toward native topology, aiding in understanding protein folding intermediates and oxidative folding pathways.

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

Benjamin Widom (1930-2024) and the "∫" : Physical Chemist, Theorist, and Mentor.

The protein journal·2026
Same author

Molecular Stability as a Translational Gate: A Structured Framework for Target Validation in Genetic Cardiomyopathy.

Cureus·2026
Same author

Biomarkers for targeted therapy and treatment decision making.

Advances in cancer research·2026
Same author

Disrupting pegRNA intramolecular complementarity via PBS and spacer sequence alterations can enhance prime editing efficiency.

Nucleic acids research·2026
Same author

PFDA Influences the Structure of the Globular Milk Protein, α-Lactalbumin: Implications for Its Ability to Bind a Physiologically Crucial Cofactor.

Chemical research in toxicology·2026
Same author

Drug Polymer Nanoparticles: An Advancement in Biomedical Solutions and Targeted Drug Delivery.

Drug design, development and therapy·2026

Area of Science:

  • Biochemistry
  • Protein Folding
  • Biophysical Chemistry

Background:

  • Protein folding is crucial for biological function.
  • Understanding oxidative folding pathways and intermediates is essential.
  • Ribonuclease A (RNase A) is a model protein for folding studies.

Purpose of the Study:

  • To characterize folding intermediates and oxidative folding processes of RNase A.
  • To investigate the nature of residual structure in early folding stages.
  • To structurally characterize oxidative folding intermediates via disulfide pairing.

Main Methods:

  • Utilized a novel method based on trans-[Pt(en)(2)Cl(2)](2+) oxidation of cysteine residues.
  • Applied this method to study RNase A under varying denaturing conditions (4-6 M GdnHCl).

Related Experiment Videos

  • Assessed the propensity for native disulfide bond formation in unfolded, reduced RNase A.

    • Main Results:

    • Unfolded reduced RNase A showed a 10-fold increased propensity for native disulfide formation compared to denaturing conditions.
    • This suggests reduced RNase A possesses a bias toward native topology, not just a condensed coil.
    • Demonstrated structural characterization of intermediates, estimating native disulfide-containing molecules in the two-disulfide ensemble.

    Conclusions:

    • The developed method effectively reveals structured intermediates in protein oxidative folding.
    • Reduced RNase A exhibits non-random structure, biasing it towards its native conformation.
    • This approach provides insights into the mechanisms governing protein folding pathways.