Department of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003, USA.
Curr Pharm Biotechnol. 2011 Oct;12(10):1558-67. doi: 10.2174/138920111798357230.
Mass spectrometry is the method of choice for sequencing peptides and proteins and is the preferred choice for characterizing post-translational modifications (PTMs). The most commonly used dissociation method to characterize peptides (i.e. collision-induced dissociation (CID)), however, has some limitations when it comes to analyzing many PTMs. Because CID chemistry is influenced by amino acid side-chains, some modifications can alter or inhibit dissociation along the peptide backbone, thereby limiting sequence information and hindering identification of the modification site. Electron transfer dissociation (ETD) has emerged as an alternate dissociation technique that, in most cases, overcomes these limitations of CID because it is less affected by side chain chemistry. Here, we review recent applications of ETD for characterizing peptide and protein PTMs with a particular emphasis on the advantages of ETD over CID, the ways in which ETD and CID have been used in a complementary manner, and how peptide modifications can still influence ETD dissociation pathways.
质谱是用于测序肽和蛋白质的首选方法，也是用于描述翻译后修饰（PTM）的首选方法。然而，最常用于表征肽的解离方法（即碰撞诱导解离（CID）），在分析许多 PTM 时存在一些局限性。由于 CID 化学受氨基酸侧链的影响，一些修饰可以改变或抑制肽骨架上的解离，从而限制序列信息并阻碍修饰部位的鉴定。电子转移解离（ETD）已成为一种替代的解离技术，在大多数情况下，它克服了 CID 的这些限制，因为它受侧链化学的影响较小。在这里，我们回顾了 ETD 在表征肽和蛋白质 PTM 方面的最新应用，特别强调了 ETD 相对于 CID 的优势、ETD 和 CID 以互补方式使用的方式，以及肽修饰如何仍然影响 ETD 解离途径。
