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

Searching for geometric molecular shape complementarity using bidimensional surface profiles.

A Badel1, J P Mornon, S Hazout

  • 1Unité de Recherches Biomathématiques et Biostatistiques, Université Paris 7, France.

Journal of Molecular Graphics
|December 1, 1992
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

Combined assessment of DYRK1A, BDNF and homocysteine levels as diagnostic marker for Alzheimer's disease.

Translational psychiatry·2017
Same author

Extraction of melodies in behavioural sequences.

Behavioural processes·2014
Same author

A new simple asymmetric hysteresis operator and its application to inverse control of piezoelectric actuators.

IEEE transactions on ultrasonics, ferroelectrics, and frequency control·2008
Same author

"Pinning strategy": a novel approach for predicting the backbone structure in terms of protein blocks from sequence.

Journal of biosciences·2007
Same author

Protein Peeling 2: a web server to convert protein structures into series of protein units.

Nucleic acids research·2006
Same author

'Hybrid protein model' for optimally defining 3D protein structure fragments.

Bioinformatics (Oxford, England)·2003
Same journal

HOLE: a program for the analysis of the pore dimensions of ion channel structural models.

Journal of molecular graphics·1996
Same journal

Analytically defined surfaces to analyze molecular interaction properties.

Journal of molecular graphics·1996
Same journal

Prediction of high-frequency electron paramagnetic resonance spectra of spin S = 3/2, 5/2 systems.

Journal of molecular graphics·1996
Same journal

Affecting the activity of soybean lipoxygenase-1.

Journal of molecular graphics·1996
Same journal

Why spin = 1, 2 species have no electron paramagnetic resonance signal under normal conditions: possible detection by electron paramagnetic resonance at frequency close to D value?

Journal of molecular graphics·1996
Same journal

Knowledge-based modeling of a legume lectin and docking of the carbohydrate ligand: the Ulex europaeus lectin I and its interaction with fucose.

Journal of molecular graphics·1996
See all related articles

This study introduces a novel 2D method for matching molecular surface sections using angular profiles. The technique efficiently aligns shapes, proving effective for protein complexes like kallikreine A-trypsin.

Area of Science:

  • Computational chemistry
  • Structural biology
  • Bioinformatics

Background:

  • Understanding molecular surface complementarity is crucial for drug discovery and protein interaction studies.
  • Existing methods may lack efficiency or precision in analyzing complex molecular shapes.

Purpose of the Study:

  • To develop and validate a novel bidimensional (2D) computational methodology for assessing molecular surface complementarity.
  • To establish an efficient approach for optimal matching of molecular surface sections.

Main Methods:

  • Describing molecular surface sections using a shape vector (angular profile).
  • Comparing angular profiles to find matching patterns.
  • Optimizing relative positions in 2D space via geometric rotations and translations.

Related Experiment Videos

Main Results:

  • Successfully demonstrated the methodology on the kallikreine A-trypsin pancreatic bovine 2 complex.
  • Achieved satisfying results in matching the two molecular surface sections.
  • The method provides a set of optimal configurations visualized on screen.

Conclusions:

  • The developed 2D approach offers an efficient method for molecular surface matching.
  • This technique can serve as a valuable preprocessing step for 3D complementarity analyses.
  • Potential applications in structural biology and computational drug design.