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Conformational Angles Database (CADB-3.0)

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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:

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

Document Type: Research Article

Publication date: 2007-07-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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