Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India.
School of Advanced Sciences, Vellore Institute of Technology, Vellore, Tamil Nadu, India.
Bioinformatics. 2020 Jun 1;36(11):3615-3617. doi: 10.1093/bioinformatics/btaa141.
Protein-carbohydrate interactions perform several cellular and biological functions and their structure and function are mainly dictated by their binding affinity. Although plenty of experimental data on binding affinity are available, there is no reliable and comprehensive database in the literature.
We have developed a database on binding affinity of protein-carbohydrate complexes, ProCaff, which contains 3122 entries on dissociation constant (Kd), Gibbs free energy change (ΔG), experimental conditions, sequence, structure and literature information. Additional features include the options to search, display, visualization, download and upload the data.
The database is freely available at http://web.iitm.ac.in/bioinfo2/procaff/. The website is implemented using HTML and PHP and supports recent versions of major browsers such as Chrome, Firefox, IE10 and Opera.
Supplementary data are available at Bioinformatics online.
蛋白质-碳水化合物相互作用具有多种细胞和生物学功能,其结构和功能主要由其结合亲和力决定。尽管有大量关于结合亲和力的实验数据,但文献中没有可靠和全面的数据库。
我们开发了一个关于蛋白质-碳水化合物复合物结合亲和力的数据库 ProCaff,其中包含 3122 个关于离解常数 (Kd)、吉布斯自由能变化 (ΔG)、实验条件、序列、结构和文献信息的条目。其他功能包括搜索、显示、可视化、下载和上传数据的选项。
该数据库可在 http://web.iitm.ac.in/bioinfo2/procaff/ 免费获得。该网站使用 HTML 和 PHP 实现,并支持 Chrome、Firefox、IE10 和 Opera 等主流浏览器的最新版本。
补充数据可在 Bioinformatics 在线获得。