Abstract
Transitions in amino-acid conformation angles tend to accompany various structural modifications in protein structures. Thus, to benefit the modeling of protein structures, the Conformation Angles DataBase (CADB-3.0) has been updated to visualize the conformational angles in varied regions (fully, generously, additionally and disallowed regions). In addition, options are provided to display the angles in the secondary structural elements (α-helix, β-sheet and 310-helix) of the Ramachandran plot. The database is being updated periodically and can be accessed over the World Wide Web at the following URL: http://cluster.physics.iisc.ernet.in/cadb/.
Keywords: Conformation angles, non-redundant protein structures, knowledgebase, allowed and disallowed regions
Protein & Peptide Letters
Title: Conformational Angles Database (CADB-3.0)
Volume: 14 Issue: 7
Author(s): K. Gopalakrishnan, S. S. Sheik, C. Vasuki Ranjani, A. Udayakumar and K. Sekar
Affiliation:
Keywords: Conformation angles, non-redundant protein structures, knowledgebase, allowed and disallowed regions
Abstract: Transitions in amino-acid conformation angles tend to accompany various structural modifications in protein structures. Thus, to benefit the modeling of protein structures, the Conformation Angles DataBase (CADB-3.0) has been updated to visualize the conformational angles in varied regions (fully, generously, additionally and disallowed regions). In addition, options are provided to display the angles in the secondary structural elements (α-helix, β-sheet and 310-helix) of the Ramachandran plot. The database is being updated periodically and can be accessed over the World Wide Web at the following URL: http://cluster.physics.iisc.ernet.in/cadb/.
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Cite this article as:
K. Gopalakrishnan , S. S. Sheik , C. Vasuki Ranjani , A. Udayakumar and K. Sekar , Conformational Angles Database (CADB-3.0), Protein & Peptide Letters 2007; 14 (7) . https://dx.doi.org/10.2174/092986607781483930
DOI https://dx.doi.org/10.2174/092986607781483930 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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