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

Protein structural domain identification.

W R Taylor1

  • 1Division of Mathematical Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London, UK.

Protein Engineering
|May 11, 1999
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

Can tibio-femoral kinematic and kinetic parameters reveal poor functionality and underlying deficits after total knee replacement? A systematic review.

The Knee·2021
Same author

In Vivo Elongation Patterns of the Collateral Ligaments in Healthy Knees During Functional Activities.

The Journal of bone and joint surgery. American volume·2021
Same author

Length-Change Patterns of the Collateral Ligaments During Functional Activities After Total Knee Arthroplasty.

Annals of biomedical engineering·2020
Same author

Author Correction: Tibio-Femoral Contact Force Distribution is Not the Only Factor Governing Pivot Location after Total Knee Arthroplasty.

Scientific reports·2019
Same author

Tibio-Femoral Contact Force Distribution is Not the Only Factor Governing Pivot Location after Total Knee Arthroplasty.

Scientific reports·2019
Same author

Analysis of the role of GSK3 in the mitotic checkpoint.

Scientific reports·2018
Same journal

pH-responsive polymer-assisted refolding of urea- and organic solvent-denatured alpha-chymotrypsin.

Protein engineering·2004
Same journal

Evaluation of different linker regions for multimerization and coupling chemistry for immobilization of a proteinaceous affinity ligand.

Protein engineering·2004
Same journal

Recombinant porcine intestinal carboxylesterase: cloning from the pig liver esterase gene by site-directed mutagenesis, functional expression and characterization.

Protein engineering·2004
Same journal

Periplasmic expression of human growth hormone via plasmid vectors containing the lambdaPL promoter: use of HPLC for product quantification.

Protein engineering·2004
Same journal

Shift of fibril-forming ability of the designed alpha-helical coiled-coil peptides into the physiological pH region.

Protein engineering·2004
Same journal

Modified peptide selection in vitro by introduction of a protein-RNA interaction.

Protein engineering·2004
See all related articles

A new method defines protein structural domains using only alpha-carbon data. This fast, simple approach accurately identifies domains and can compare multiple protein structures simultaneously.

Area of Science:

  • Structural biology
  • Computational biology
  • Bioinformatics

Background:

  • Protein structural domains are fundamental units of protein architecture.
  • Accurate domain definition is crucial for understanding protein function and evolution.
  • Existing methods may require extensive data or lack flexibility.

Purpose of the Study:

  • To develop a simple and efficient method for defining protein structural domains.
  • To improve the accuracy of domain identification, particularly for beta-sheet structures.
  • To enable simultaneous domain definition across related protein structures.

Main Methods:

  • Utilizes only alpha-carbon coordinate data for domain definition.
  • Incorporates a bias for beta-sheet integrity and an acceptance condition.

Related Experiment Videos

  • Employs an automatically adjusted granularity parameter based on native and smoothed structures.
  • Extends to simultaneous domain definition across multiple related structures without averaging.

    • Main Results:

    • The method accurately captures the essence of most protein domains.
    • It shows improved handling of beta-sheet structure integrity.
    • Automatic granularity adjustment successfully separates tightly packed domains.
    • Comparison with existing definitions shows high-quality, largely correct results.
    • Simultaneous domain definition effectively reconciles structural differences in families.

    Conclusions:

    • This simple, fast method provides accurate protein domain definitions.
    • It offers a robust approach for analyzing protein structural families.
    • The technique is broadly applicable in structural biology and bioinformatics.