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Related Experiment Videos

Conformational Angles DataBase (CADB-3.0).

K Gopalakrishnan1, S S Sheik, C Vasuki Ranjani

  • 1Bioinformatics Centre (Centre of Excellence in Structural Biol. & Bio-comput.), Indian Institute of Science, Bangalore 560 012, India.

Protein and Peptide Letters
|September 28, 2007
PubMed
Summary
This summary is machine-generated.

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The Conformation Angles DataBase (CADB-3.0) now visualizes amino-acid angles in protein structures, aiding in better protein modeling and understanding structural modifications.

Area of Science:

  • Structural Biology
  • Bioinformatics

Background:

  • Amino-acid conformation angles are crucial for understanding protein structure.
  • Changes in these angles correlate with significant structural modifications in proteins.
  • Accurate modeling of protein structures relies on detailed conformational data.

Purpose of the Study:

  • To update and enhance the Conformation Angles DataBase (CADB-3.0).
  • To provide visualization tools for conformational angles in proteins.
  • To aid in the modeling and analysis of protein structures.

Main Methods:

  • Updated the Conformation Angles DataBase (CADB-3.0).
  • Implemented visualization of conformational angles across different regions (fully, generously, additionally, disallowed).
  • Enabled display of angles within specific secondary structural elements (alpha-helix, beta-sheet, 3(10)-helix) on the Ramachandran plot.

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Main Results:

  • CADB-3.0 now offers enhanced visualization of amino-acid conformational angles.
  • The database categorizes angles into distinct regions for clearer analysis.
  • Conformational angles can be viewed within specific secondary structures.

Conclusions:

  • The updated CADB-3.0 database improves the visualization of protein conformational angles.
  • This resource facilitates a deeper understanding of protein structure and modifications.
  • The database is a valuable tool for protein structure modeling and research.