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

Exploring protein sequence space using knowledge-based potentials.

A Babajide1, R Farber, I L Hofacker

  • 1Institut für Theoretische Chemie und Molekulare Strukturbiologie, Universität Wien, Währingerstrasse 17, A-1090 Vienna, Austria.

Journal of Theoretical Biology
|August 31, 2001
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

The effects of biostimulation and bioaugmentation on crude oil biodegradation in two adjacent terrestrial oil spills of different age, in a hyper-arid region.

Journal of environmental management·2021
Same author

Tracing the evolution of the heterotrimeric G protein α subunit in Metazoa.

BMC evolutionary biology·2018
Same author

Hidden treasures in unspliced EST data.

Theory in biosciences = Theorie in den Biowissenschaften·2012
Same author

Identification and classification of small RNAs in transcriptome sequence data.

Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing·2009
Same author

Sequence assembly.

Computational biology and chemistry·2009
Same author

RNA structures with pseudo-knots: graph-theoretical, combinatorial, and statistical properties.

Bulletin of mathematical biology·2007
Same journal

The male-biased sex ratio in humans and its role in the transition from promiscuity to pair bonding.

Journal of theoretical biology·2026
Same journal

Quantifying the counter-intuitive effects of vaccination by coupling the transmission dynamics of COVID-19 and the evolution of human behaviors.

Journal of theoretical biology·2026
Same journal

An integrative model of FGF2-induced signaling and muscle cell proliferation.

Journal of theoretical biology·2026
Same journal

A hybrid reaction-diffusion and mechanical stimulus model for mandibular bone remodeling under chewing and vibratory loading.

Journal of theoretical biology·2026
Same journal

Integrated tick management strategies in fragmented peridomestic environments.

Journal of theoretical biology·2026
Same journal

Joint likelihood-free inference of the number of selected single nucleotide polymorphisms and their selection coefficients in an evolving population.

Journal of theoretical biology·2026
See all related articles

This study explores protein sequence-structure relationships. Computer simulations show that protein folds form extensive neutral networks, suggesting evolutionary pathways are robust and interconnected.

Area of Science:

  • Computational biology
  • Protein structure prediction
  • Evolutionary bioinformatics

Background:

  • Knowledge-based potentials guide protein folding predictions.
  • Understanding sequence-structure relationships is crucial for evolutionary studies.
  • Neutral networks are hypothesized to facilitate efficient evolution.

Purpose of the Study:

  • To survey sequence-structure relations in protein space.
  • To test if protein sequences for a specific fold form extensive neutral networks.
  • To determine if neutral networks of different folds are closely interconnected.

Main Methods:

  • Utilized knowledge-based potentials to assess sequence-structure compatibility.
  • Employed computer simulations to analyze protein sequence space.

Related Experiment Videos

  • Tested two distinct potential functions: PROSA pair potential and a neural network potential.
  • Main Results:

    • Confirmed that sequences for a given native fold form extensive, percolating neutral networks.
    • Demonstrated that neutral networks of different native folds are proximate, within a few mutations.
    • Validated these findings using two different computational potential functions.

    Conclusions:

    • Protein sequence space is organized around large neutral networks facilitating evolution.
    • The proximity of neutral networks supports the idea of evolutionary pathways readily switching between folds.
    • Computational potentials effectively probe sequence-structure landscapes and evolutionary propositions.