Department of Molecular Biology, Princeton University, Princeton, NJ 08540, U.S.A.
Essays Biochem. 2012;52:147-63. doi: 10.1042/bse0520147.
The complexity of an organism's proteome is in part due to the diversity of post-translational modifications present that can direct the location and function of a protein. To address the growing interest in characterizing these modifications, mass spectrometric-based proteomics has emerged as one of the most essential experimental platforms for their discovery. In searching for post-translational modifications within a target set of proteins to global surveys of particularly modified proteins within a given proteome, various experimental MS (mass spectrometry) and allied techniques have been developed. Out of 20 naturally encoded amino acids, lysine is essentially the most highly post-translationally modified residue. This chapter provides a succinct overview of such methods for the characterization of protein lysine modifications as broadly classified, such as methylation and ubiquitination.
蛋白质组的复杂性部分归因于存在的翻译后修饰的多样性，这些修饰可以指导蛋白质的位置和功能。为了解决对这些修饰进行描述的日益增长的兴趣，基于质谱的蛋白质组学已成为发现这些修饰的最基本的实验平台之一。在寻找目标蛋白质组中特定修饰的蛋白质的翻译后修饰时，已经开发了各种实验 MS（质谱）和相关技术。在 20 种天然编码的氨基酸中，赖氨酸基本上是被翻译后修饰最多的残基。本章简要概述了广泛分类的蛋白质赖氨酸修饰的这种特征描述方法，例如甲基化和泛素化。
