期刊
ANALYTICAL CHEMISTRY
卷 82, 期 1, 页码 28-31出版社
AMER CHEMICAL SOC
DOI: 10.1021/ac902134y
关键词
-
资金
- Princeton University
- National Science Foundation [CBET-0941143]
- Waters Corporation
Covalent adenosine diphosphate (ADP)-ribosylation of proteins is a post-translational modification that can occur both enzymatically and nonenzymatically and has been linked to many biological processes, such as the DNA damage and response mechanisms. Although the biochemistry of protein ADP-ribosylation has been extensively studied, the identification of physiological substrates remains a significant challenge due to inadequate tools for characterizing these modified peptides. Here we show that the use of electron transfer dissociation (EM) greatly simplifies the mass spectrometric (MS) sequencing of ADP-ribosylated peptides over the conventional collisionally activated dissociation (CAD) approach. ETD sequencing of ADP-ribosylated peptides can be performed within a time scale compatible with nanoflow liquid chromatography and should prove useful for high-throughput large-scale studies on this unique class of modified peptides.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据