A collision cross-section database of singly-charged peptide ions
A collision cross-section database of singly-charged peptide ions
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DOI：
10.1016/j.jasms.2007.04.003
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发表时间：
2007-07-01
影响因子：
3.2
通讯作者：
Russell, David H.
中科院分区：
文献类型：
--
作者：
Tao, Lei;McLean, Janel R.;Russell, David H.
建立了单电荷肽离子中性碰撞截面数据库。数据库中包含的肽是通过使用三种不同的酶对已知蛋白质进行酶消化而产生的，从而产生在氨基酸组成以及N-末端和C-末端残基方面不同的肽。使用直接耦合到飞行时间（TOF）质谱仪的离子迁移率（IM）光谱法测量离子-中性碰撞截面。离子由基质辅助激光解吸电离（MALDI）离子源形成，该离子源在2至3埃的压力（He浴气体）下操作。大多数（63%）的肽离子碰撞横截面与最好描述为电荷溶剂化小球的结构相关，但大量的肽离子表现出的碰撞横截面显着大于或小于平均，球状迁移率-质量相关性。在具有大于平均碰撞横截面的肽离子中，类似于71%来自胰蛋白酶消化（C-末端Arg或Lys残基），并且大多数具有较小（比球形）碰撞横截面的肽离子来自胃蛋白酶消化（90%）。
A database of ion-neutral collision cross-sections for singly-charged peptide ions is presented. The peptides included in the database were generated by enzymatic digestion of known proteins using three different enzymes, resulting in peptides that differ in terms of amino acid composition as well as N-terminal and C-terminal residues. The ion-neutral collision cross-sections were measured using ion mobility (IM) spectrometry that is directly coupled to a time-of-flight (TOF) mass spectrometer. The ions were formed by a matrix-assisted laser desorption ionization (MALDI) ion source operated at pressures (He bath gas) of 2 to 3 torr. The majority (63%) of the peptide ion collision cross-sections correlate well with structures that are best described as charge-solvated globules, but a significant number of the peptide ions exhibit collision cross-sections that are significantly larger or smaller than the average, globular mobility-mass correlation. Of the peptide ions having larger than average collision cross-sections, similar to 71% are derived from trypsin digestion (C-terminal Arg or Lys residues) and most of the peptide ions that have smaller (than globular) collision cross-sections are derived from pepsin digestion (90%).