Laimer Josef, Hiebl-Flach Julia, Lengauer Daniel, Lackner Peter
Department of Molecular Biology, University of Salzburg, Salzburg 5020 School of Informatics, Communications and Media, University of Applied Sciences Upper Austria, Hagenberg 4232, Austria.
School of Informatics, Communications and Media, University of Applied Sciences Upper Austria, Hagenberg 4232, Austria.
Bioinformatics. 2016 May 1;32(9):1414-6. doi: 10.1093/bioinformatics/btv769. Epub 2016 Jan 6.
The prediction of change in stability upon point mutations in proteins has many applications in protein analysis and engineering. We recently adjoined a new structure-based method called MAESTRO, which is distributed as command line program. We now provide access to the most important features of MAESTRO by an easy to use web service. MAESTROweb allows the prediction of change in stability for user-defined mutations, provides a scan functionality for the most (de)stabilizing n-point mutations for a maximum of n = 5, creates mutation sensitivity profiles and evaluates potential disulfide bonds. MAESTROweb operates on monomers, multimers and biological assemblies as defined by PDB.
MAESTROweb is freely available for non-commercial use at https://biwww.che.sbg.ac.at/maestro/web
预测蛋白质点突变后稳定性的变化在蛋白质分析和工程中有许多应用。我们最近采用了一种名为MAESTRO的新的基于结构的方法,它作为命令行程序分发。现在,我们通过一个易于使用的网络服务提供对MAESTRO最重要功能的访问。MAESTROweb允许预测用户定义突变的稳定性变化,为最多n = 5的最(去)稳定n点突变提供扫描功能,创建突变敏感性图谱并评估潜在的二硫键。MAESTROweb可处理由PDB定义的单体、多聚体和生物组装体。
MAESTROweb可在https://biwww.che.sbg.ac.at/maestro/web上免费用于非商业用途。