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基质辅助激光解吸电离源内裂解质谱法对同型亮氨酸/异亮氨酸残基的鉴别。

Discrimination of isobaric Leu/Ile residues by MALDI in-source decay mass spectrometry.

机构信息

Chemistry Department and GIGA-R, Mass Spectrometry Laboratory, University of Liege, Liege, Belgium.

出版信息

J Am Soc Mass Spectrom. 2013 Feb;24(2):297-300. doi: 10.1007/s13361-012-0523-7. Epub 2013 Jan 11.

DOI:10.1007/s13361-012-0523-7
PMID:23307320
Abstract

MALDI in-source decay (ISD) has been used for top-down sequencing of proteins. The use of the matrix 1,5-diaminonapthalene (1,5-DAN) gave abundant w ions, which are formed from the unimolecular dissociation of z• radical fragments via α cleavage reaction and thus help identify which of the isobaric amino acids, Leu or Ile, is present. The high abundance of w ions in MALDI-ISD with 1,5-DAN results from the low collision rate in the MALDI plume. MALDI-ISD with 1,5-DAN appears to be an useful method for the top-down sequencing of proteins, including discrimination of Leu and Ile near the C-terminal end.

摘要

基质辅助激光解吸电离源内裂解(MALDI-ISD)已被用于蛋白质的从头测序。使用基质 1,5-二氨基萘(1,5-DAN)可产生丰富的 w 离子,这些离子是通过α断裂反应从 z•自由基碎片的单分子解离形成的,因此有助于确定存在的是等摩尔的氨基酸亮氨酸或异亮氨酸。在 MALDI 羽流中低碰撞速率导致用 1,5-DAN 进行 MALDI-ISD 时,w 离子的丰度很高。对于包括靠近 C 末端的亮氨酸和异亮氨酸的区分在内的蛋白质从头测序,MALDI-ISD 与 1,5-DAN 结合似乎是一种有用的方法。

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Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.激进解决方案:基于电子的离解在基于质谱的蛋白质结构分析中的原理和应用。
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