| Literature DB >> 17897091 |
K Gopalakrishnan1, S S Sheik, C Vasuki Ranjani, A Udayakumar, K Sekar.
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 (alpha-helix, beta-sheet and 3(10)-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/.Mesh:
Year: 2007 PMID: 17897091 DOI: 10.2174/092986607781483930
Source DB: PubMed Journal: Protein Pept Lett ISSN: 0929-8665 Impact factor: 1.890