APPLICATION OF PTMAP2 FOR PROTEIN POSTTRANSLATIONAL MODIFICATION ANALYSIS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 翻译后修饰(PTM)在蛋白质功能和细胞生理中起着至关重要的作用。利用质谱学对所有类型的PTMS进行无限制的鉴定是一种强有力的方法。之前的努力使我们成功地开发了PTMap v2.0，这是一种用于蛋白质翻译后修饰的全基因组表征的工具。初步测试表明，PTMap2能够从单一的质谱学数据文件中识别大肠杆菌蛋白质数据库中的所有类型的PTM。在这里，我们建议扩大PTMap2工具的应用范围，以识别不同细胞生物中的未知PTM。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Posttranslational modifications (PTMs) play essential roles in protein function and cellular physiology. Unrestrictive identification of all types of PTMs using mass spectrometry is a powerful approach. Previous efforts have allowed us to successfully develop PTMap v2.0, a tool for genome-wide characterization of protein posttranslational modifications. Initial tests demonstrate that PTMap2 is capable to identify all types of PTMs in E. coli protein database from a single mass spectrometry data file. Here we propose to extend the application of PTMap2 tool to identify unknown PTMs in diverse cellular organisms.