Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan.
Nucleic Acids Res. 2012 Jan;40(Database issue):D507-11. doi: 10.1093/nar/gkr884. Epub 2011 Nov 8.
IDEAL, Intrinsically Disordered proteins with Extensive Annotations and Literature (http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/), is a collection of knowledge on experimentally verified intrinsically disordered proteins. IDEAL contains manual annotations by curators on intrinsically disordered regions, interaction regions to other molecules, post-translational modification sites, references and structural domain assignments. In particular, IDEAL explicitly describes protean segments that can be transformed from a disordered state to an ordered state. Since in most cases they can act as molecular recognition elements upon binding of partner proteins, IDEAL provides a data resource for functional regions of intrinsically disordered proteins. The information in IDEAL is provided on a user-friendly graphical view and in a computer-friendly XML format.
IDEAL，即具有广泛注释和文献的内在无序蛋白质（http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/），是一个经过实验验证的内在无序蛋白质知识库。IDEAL 包含由管理员手动注释的内在无序区域、与其他分子的相互作用区域、翻译后修饰位点、参考文献和结构域分配。特别是，IDEAL 明确描述了可以从无序状态转变为有序状态的蛋白质片段。由于在大多数情况下，它们可以在与伴侣蛋白结合时充当分子识别元件，因此 IDEAL 为内在无序蛋白质的功能区域提供了数据资源。IDEAL 中的信息以用户友好的图形视图和计算机友好的 XML 格式提供。
