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

A designed heterotrimeric coiled coil

S Nautiyal1, D N Woolfson, D S King

  • 1Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.

Biochemistry
|September 19, 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

Labile assembly of a tardigrade protein induces biostasis.

Protein science : a publication of the Protein Society·2024
Same author

Perceptions of change in the environment caused by the COVID-19 pandemic: Implications for environmental policy.

Environmental impact assessment review·2022
Same author

Effects of Reduced Training on Muscular Power in Swimmers.

The Physician and sportsmedicine·2016
Same author

A-Z of nutritional supplements: dietary supplements, sports nutrition foods and ergogenic aids for health and performance-Part 34.

British journal of sports medicine·2012
Same author

Non-Tuberculous Miliary Lesions of the Lung.

Transactions of the American Clinical and Climatological Association·2011
Same author

Can We Cure Tuberculosis by Cutting Out the Necrotic Foci.

Transactions of the American Clinical and Climatological Association·2011
Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026
Same journal

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Biochemistry·2026
Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026
Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026
Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026
See all related articles

Scientists designed three peptides to form a stable, specific coiled coil trimer. This validates design principles for creating self-assembling protein structures.

Area of Science:

  • Protein structure and design
  • Biochemistry
  • Molecular biology

Background:

  • Coiled coils are protein structures formed by alpha-helices.
  • Designing specific protein-protein interactions is crucial for synthetic biology.

Purpose of the Study:

  • To test principles for guiding coiled coil folding.
  • To design peptides that form a specific heterotrimeric coiled coil.

Main Methods:

  • Designed three peptides with core residues promoting trimer formation.
  • Utilized ionic interactions for heterospecificity and negative design.
  • Developed a program to optimize interhelical interactions and minimize alternative structures.

Main Results:

  • Solution studies confirmed the formation of a helical trimer from an equimolar peptide mixture.

Related Experiment Videos

  • The heterotrimer exhibited high specificity and stability.
  • The designed peptides successfully formed the intended parallel heterotrimeric coiled coil.

    • Conclusions:

    • The study validates the design principles for creating specific coiled coil structures.
    • The designed heterotrimer can potentially serve as an autonomous trimerization domain.
    • This work demonstrates the feasibility of de novo protein design for specific quaternary structures.