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

FROST: a filter-based fold recognition method.

Antoine Marin1, Joël Pothier, Karel Zimmermann

  • 1Mathématique, Informatique et Génome, Centre de Recherche de Versailles, INRA, Route de St Cyr, 78026 Versailles, Cedex, France.

Proteins
|October 29, 2002
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

Development of an Instrumented Glove for Palmar Pressure Assessment in Kayakers.

Sensors (Basel, Switzerland)·2026
Same author

Motor patterns of the impaired upper limb in children with unilateral cerebral palsy performing bimanual tasks.

Clinical biomechanics (Bristol, Avon)·2022
Same author

Are Virulence and Antibiotic Resistance Genes Linked? A Comprehensive Analysis of Bacterial Chromosomes and Plasmids.

Antibiotics (Basel, Switzerland)·2022
Same author

A Minimal yet Flexible Likelihood Framework to Assess Correlated Evolution.

Systematic biology·2021
Same author

The Perfect Condition for the Rising of Superbugs: Person-to-Person Contact and Antibiotic Use Are the Key Factors Responsible for the Positive Correlation between Antibiotic Resistance Gene Diversity and Virulence Gene Diversity in Human Metagenomes.

Antibiotics (Basel, Switzerland)·2021
Same author

A new child-friendly 3D bimanual protocol to assess upper limb movement in children with unilateral cerebral palsy: Development and validation.

Journal of electromyography and kinesiology : official journal of the International Society of Electrophysiological Kinesiology·2020

We developed FROST (Fold Recognition-Oriented Search Tool), a novel protein fold assignment method. FROST achieves 60% coverage with a 1% error rate, outperforming existing tools like PSI-BLAST and 3D-PSSM in realistic fold recognition benchmarks.

Area of Science:

  • Computational Biology
  • Structural Bioinformatics
  • Protein Science

Background:

  • Accurate protein fold assignment is crucial for understanding protein function and evolution.
  • Existing fold recognition methods face challenges in realistic scenarios with low sequence similarity.
  • Developing robust benchmarks is essential for evaluating fold recognition tools.

Purpose of the Study:

  • To develop and assess a novel fold recognition method, FROST (Fold Recognition-Oriented Search Tool).
  • To create a specialized benchmark database for realistic evaluation of fold recognition tools.
  • To compare FROST's performance against established methods like PSI-BLAST and 3D-PSSM.

Main Methods:

  • FROST utilizes a series of filters and a custom-designed benchmark database.

Related Experiment Videos

  • The benchmark database includes protein pairs with high structural similarity (>65% residue alignment) but no detectable sequence similarity.
  • Performance was evaluated based on coverage at a 1% error rate.

    • Main Results:

    • FROST achieved 60% coverage at a 1% error rate.
    • PSI-BLAST achieved 33% coverage and 3D-PSSM achieved 56% coverage under identical conditions.
    • FROST demonstrates superior performance in identifying protein folds with low sequence similarity.

    Conclusions:

    • FROST is a reliable and effective method for protein fold assignment, particularly in challenging cases.
    • The developed benchmark database provides a realistic assessment of fold recognition tool performance.
    • FROST offers a significant improvement over existing methods for identifying protein structural relationships.