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

ProSup: a refined tool for protein structure alignment.

P Lackner1, W A Koppensteiner, M J Sippl

  • 1Center for Applied Molecular Engineering, Institute for Chemistry and Biochemistry, University of Salzburg, Jakob-Haringer Str. 3, A-5020 Salzburg, Austria.

Protein Engineering
|February 13, 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

Behavioral characterization of the anterior injection model of subarachnoid hemorrhage.

Behavioural brain research·2017
Same author

Clusters of cortical spreading depolarizations in a patient with intracerebral hemorrhage: a multimodal neuromonitoring study.

Neurocritical care·2014
Same author

Differences in the intrinsic immunogenicity and allergenicity of Bet v 1 and related food allergens revealed by site-directed mutagenesis.

Allergy·2013
Same author

Cerebral vasospasm following temporal lobe epilepsy surgery.

Neurology·2012
Same author

Recurrent intracerebral haemorrhage after coitus: a case report of sporadic cerebral amyloid angiopathy in a younger patient.

European journal of neurology·2012
Same author

Identification of B-cell epitopes of Bet v 1 involved in cross-reactivity with food allergens.

Allergy·2009
Same journal

Structure of a human Rhinovirus complexed with its receptor molecule.

Protein engineering·2024
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
See all related articles

This study optimized a protein structure comparison method using rigid body superposition. The method effectively identifies structurally similar proteins and ranks database searches, aligning with expert classifications.

Area of Science:

  • Structural bioinformatics
  • Computational biology
  • Biochemistry

Background:

  • Protein structure comparison is crucial for understanding function and evolution.
  • Existing methods may struggle with detecting remote structural similarities.
  • Identifying structurally equivalent residues is key to accurate comparison.

Purpose of the Study:

  • To optimize a novel method for protein structure comparison.
  • To establish a robust similarity measure based on equivalent residues.
  • To evaluate the method's ability to detect remote similarities and rank database searches.

Main Methods:

  • Rigid body superposition for aligning protein structures.
  • Maximizing structurally equivalent residues while maintaining constant root mean square deviation.

Related Experiment Videos

  • Utilizing the number of equivalent residues as a similarity metric.
  • Main Results:

    • The optimized method successfully detects remote structural similarity.
    • The number of equivalent residues serves as an effective similarity measure.
    • Results show strong agreement with expert protein structure classifications.
    • The method provides multiple alternative alignments, reflecting the complexity of structure comparison.

    Conclusions:

    • The developed method offers an interpretable and effective approach for protein structure comparison.
    • It is suitable for ranking large-scale database searches.
    • The ability to identify multiple solutions enhances the understanding of structural relationships.