Gopalakrishnan K, Sheik S S, Ranjani C Vasuki, Udayakumar A, Sekar K
Bioinformatics Centre (Centre of Excellence in Structural Biol. & Bio-comput.), Indian Institute of Science, Bangalore 560 012, India.
Protein Pept Lett. 2007;14(7):665-8. doi: 10.2174/092986607781483930.
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/.
氨基酸构象角的转变往往伴随着蛋白质结构的各种结构修饰。因此，为了有助于蛋白质结构的建模，构象角数据库（CADB - 3.0）已更新，以可视化不同区域（完全允许、宽松允许、额外允许和禁止区域）的构象角。此外，还提供了在拉氏图的二级结构元件（α - 螺旋、β - 折叠和3(10)-螺旋）中显示角度的选项。该数据库会定期更新，可通过以下网址在万维网上访问：http://cluster.physics.iisc.ernet.in/cadb/ 。
