Ion mobility-mass spectrometry: a new paradigm for proteomics
Ion mobility-mass spectrometry: a new paradigm for proteomics
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DOI：
10.1016/j.ijms.2004.10.003
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发表时间：
2005-02-01
影响因子：
1.8
通讯作者：
Russell, DH
中科院分区：
文献类型：
--
作者：
McLean, JA;Ruotolo, BT;Russell, DH
基质辅助激光解吸/电离 (MALDI) 与离子淌度质谱 (IM-MS) 相结合，为复杂生物样品（例如肽、寡核苷酸、糖缀合物、脂质等）的二维 (2D) 分离、阐明无溶剂二级结构元素提供了一种快速方法 （如螺旋、β-发夹、随机卷曲等）、快速鉴定小分子的翻译后修饰（如磷酸化、糖基化等）或连接，以及生物聚合物的同步全面测序信息。在 IM-MS 中，蛋白质鉴定信息由结构表征数据补充。这是使用传统的蛋白质组学技术很难获得的。提高品质因数（例如灵敏度、检测限、动态范围和分析物选择性）和优化 IM-MS 实验参数的新途径。在蛋白质组学研究前沿获取新信息的背景下进行描述。 (C) 2004 Elsevier B.V. 保留所有权利。
Matrix-assisted laser desorption/ionization (MALDI) coupled with ion mobility-mass spectrometry, (IM-MS) provide's a rapid means for the two-dimensional (2D) separation of complex biological samples (e.g., peptides, oligonucleotides, glycoconjugates, lipids. etc.), elucidation of solvent-free secondary structural elements (e.g., helices, beta-hairpins, random coils, etc.), rapid identification of post-translational modifications (e.g., phosphorylation, glycosylation, etc.) or ligation of small molecules, and simultaneous and comprehensive sequencing information of biopolymers. In IM-MS, protein-identification information is complemented by structural characterization data. which is difficult to obtain using conventional proteomic techniques. New avenues for enhancing the figures of merit (e.g,. sensitivity. limits of detection, dynamic range, and analyte selectivity) and optimizing IM-MS experimental parameters are. described in the context of deriving new information at the forefront of proteomics research. (C) 2004 Elsevier B.V. All rights reserved.