利用质谱法绘制蛋白质翻译后修饰图谱。

Mapping protein post-translational modifications with mass spectrometry.

作者信息

Witze Eric S, Old William M, Resing Katheryn A, Ahn Natalie G

机构信息

Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, Colorado 80309-0215, USA.

出版信息

Nat Methods. 2007 Oct;4(10):798-806. doi: 10.1038/nmeth1100.

DOI:10.1038/nmeth1100

PMID:17901869

Abstract

Post-translational modifications of proteins control many biological processes, and examining their diversity is critical for understanding mechanisms of cell regulation. Mass spectrometry is a fundamental tool for detecting and mapping covalent modifications and quantifying their changes. Modern approaches have made large-scale experiments possible, screening complex mixtures of proteins for alterations in chemical modifications. By profiling protein chemistries, biologists can gain deeper insight into biological control. The aim of this review is introduce biologists to current strategies in mass spectrometry-based proteomics that are used to characterize protein post-translational modifications, noting strengths and shortcomings of various approaches.

摘要

蛋白质的翻译后修饰控制着许多生物学过程，研究其多样性对于理解细胞调控机制至关重要。质谱分析是检测和绘制共价修饰并量化其变化的基本工具。现代方法使大规模实验成为可能，可筛查复杂蛋白质混合物的化学修饰变化。通过分析蛋白质化学性质，生物学家能够更深入地了解生物控制。本综述的目的是向生物学家介绍基于质谱的蛋白质组学中用于表征蛋白质翻译后修饰的当前策略，并指出各种方法的优缺点。