Conformational Angles Database (CADB-3.0)

Author(s): K. Gopalakrishnan, S. S. Sheik, C. Vasuki Ranjani, A. Udayakumar, K. Sekar.

Journal Name: Protein & Peptide Letters

Volume 14 , Issue 7 , 2007

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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:

Keywords: Conformation angles, non-redundant protein structures, knowledgebase, allowed and disallowed regions

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Article Details

Year: 2007
Page: [665 - 668]
Pages: 4
DOI: 10.2174/092986607781483930
Price: $58

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