Advanced Fragmentation Methods in Biomolecular Mass Spectrometry - Probing Primary and Higher Order Structure with Electrons, Photons and Surfaces
Advanced Fragmentation Methods in Biomolecular Mass Spectrometry - Probing Primary and Higher Order Structure with Electrons, Photons and Surfaces
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生物分子质谱中的高级碎裂方法 - 用电子、光子和表面探测初级和高阶结构
DOI：
10.1039/9781839161056-00235
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发表时间：
2020
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影响因子：
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通讯作者：
Black R
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文献类型：
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作者：
Black R
碰撞诱导解离（CID）是质谱（MS）实验中用于碎片化离子的公认且卓越的方法。1这是大多数商业质谱仪的标准操作程序，具有重现性方面的显著优势，尤其是在组学应用中。2-4在经典的CID实验中，给定的分子离子被加速通过充满惰性气体的质谱仪区域。碎片化通过碰撞进行，这导致动能转移以破坏给定分析物中最弱的键。这种对较弱键的偏好可能是不利的，例如在切割翻译后修饰（PTM）中，并且当应用于非共价蛋白质复合物时，在片段化之前沉积的能量基本上扰乱三级结构。CID在自下而上的蛋白质组学研究中是常见的，其中肽离子不能提供关于蛋白质组学的信息。
The well-established and preeminent method used to fragment ions in a mass spectrometry (MS) experiment is collision-induced dissociation (CID). 1 This is a standard operating procedure in most commercial mass spectrometers with undoubted benefits in reproducibility especially in ‘omic applications. 2–4 In a classic CID experiment, a given molecular ion is accelerated through a region of the mass spectrometer filled with an inert gas. Fragmentation proceeds via collisions which results in the transfer of kinetic energy to break the weakest bonds in a given analyte. This preference for weaker bonds can be disadvantageous, for example in cleaving post-translational modifications (PTMs), and when applied to noncovalent protein complexes, the energy deposited prior to fragmentation substantially perturbs the tertiary structure. CID is common in bottom-up proteomics investigations where peptide ions cannot inform on the