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

Building a metal binding domain, one half at a time.

Sarah L J Michel1, Jeremy M Berg

  • 1Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

Chemistry & Biology
|June 25, 2002
PubMed
Summary

A specific zinc binding peptide sequence can form one stable structure alone, but changes to a different fold when it is part of a larger protein. This highlights how protein context influences peptide structure.

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

The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026
Same author

Training AI to Improve Distinction of Triple-Negative Invasive Breast Cancer from Cysts and Fibroadenomas on Ultrasound.

Diagnostics (Basel, Switzerland)·2026
Same author

A Dinuclear Iron(II) Persulfide Complex Reacts with O<sub>2</sub> to Give Sulfite: Relevance to Persulfide Dioxygenases.

Journal of the American Chemical Society·2026
Same author

How data can help to guide NIH funding policy.

Nature·2026
Same author

H<sub>2</sub>S-Mediated Persulfidation of the Classical Zinc Finger Protein Yin-Yang 1.

Biochemistry·2026
Same author

Persulfidation of the zinc finger protein ZRANB2 modulates its RNA binding and alternative splicing function.

Journal of inorganic biochemistry·2026

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Peptide structure is crucial for biological function.
  • Protein structure can influence the conformation of its constituent peptide sequences.

Purpose of the Study:

  • To investigate the structural plasticity of a specific zinc binding peptide.
  • To determine how the surrounding protein environment affects peptide folding.

Main Methods:

  • X-ray crystallography was used to determine the peptide structure.
  • Comparative structural analysis was performed on the isolated peptide and within a larger protein domain.

Main Results:

  • The zinc binding peptide adopts a distinct stable fold when isolated.

Related Experiment Videos

  • The same peptide sequence adopts an alternative stable fold when incorporated into a larger protein domain.

    • Conclusions:

    • The conformational behavior of peptides is highly dependent on their molecular context.
    • Understanding context-dependent folding is vital for protein design and function prediction.