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

Molecular dimension explored in evolution to promote proteomic complexity.

Ariel Fernández1, R Stephen Berry

  • 1Indiana University School of Informatics and Indiana Genomics Initiative Center for Computational Biology and Bioinformatics, Indiana University Medical School, 714 North Senate Avenue, Indianapolis, IN 46202, USA. arfernan@iupui.edu

Proceedings of the National Academy of Sciences of the United States of America
|September 7, 2004
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

Quantitative phase microscopy for time-lapse hypoxia-induced cellular assays based on the transport of intensity equation.

Applied optics·2025
Same author

Single-shot 3 × 3 Mueller matrix microscopy with color polarization encoding.

Optics letters·2024
Same author

Differential effects of coverslip-induced hypoxia and cobalt chloride mimetic hypoxia on cellular stress, metabolism, and nuclear structure.

Tissue & cell·2024
Same author

Spatial perception in stereoscopic augmented reality based on multifocus sensing.

Optics express·2024
Same author

Real-time phase retrieval in division of aperture microscopy with the transport of intensity equation.

Journal of the Optical Society of America. A, Optics, image science, and vision·2024
Same author

Contributions of viral oncogenes of HPV-18 and hypoxia to oxidative stress and genetic damage in human keratinocytes.

Scientific reports·2023
Same journal

Costunolide ameliorates autoimmune uveitis by targeting USP15 to suppress TNF-α-induced retinal endothelial inflammation.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

A ligandable PNT domain establishes ERG as a directly targetable oncogenic driver in prostate cancer.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Identification of cellular intermediates unveils unique enzymes for flagellar glycan biosynthesis in <i>Clostridioides difficile</i>.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

The structure of correlated variability reflects task-relevant information in sensory neurons.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Shared neurogenetic substrates of nonplanning impulsivity and procrastination.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

HIV-1 capsid interactions with Nuclear Pore Complex components support nuclear entry via affinity gradient.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Protein interaction networks evolve through mutations that alter protein structure, influencing new partnerships. Structure wrapping, or protection from water, is key to understanding how proteins gain new connections during evolution.

Area of Science:

  • Evolutionary biology
  • Structural biology
  • Systems biology

Background:

  • Protein interaction networks are fundamental to cellular processes.
  • The evolution of these networks is driven by changes in protein structure and function.
  • Gene duplication is a major driver of network expansion and complexity.

Purpose of the Study:

  • To investigate how evolution-related mutations influence protein structure to promote new protein associations.
  • To understand the mechanisms behind conserved protein folds accommodating new binding partnerships after gene duplication.
  • To elucidate the structural basis for hub proteins acquiring new connections.

Main Methods:

  • Analysis of protein structure conservation and adaptation.
  • Examination of the role of structure wrapping (protection from water) in protein interactions.

Related Experiment Videos

  • Comparative analysis of protein interaction networks and their evolutionary trajectories.

    • Main Results:

    • Protein folds can remain conserved while accommodating new binding partnerships, facilitated by specific evolutionary mutations.
    • Structure wrapping is identified as a critical factor in the acquisition of new protein connections.
    • Hub proteins, characterized by their structural properties, are more prone to evolving new interactions.

    Conclusions:

    • Evolutionary mutations shape protein structure to drive the development of complex protein interaction networks.
    • Structure wrapping is a fundamental principle governing the evolution of proteomic interactivity.
    • Understanding these principles provides insights into network dynamics and protein evolution.