化学
半胱氨酸
电子转移离解
离解(化学)
劈开
二硫键
二硫键
电子转移
电子俘获离解
劈理(地质)
硫醇
组合化学
碰撞诱导离解
离子
立体化学
光化学
有机化学
酶
生物化学
串联质谱法
质谱法
色谱法
岩土工程
断裂(地质)
工程类
傅里叶变换离子回旋共振
作者
Philippe Massonnet,Grégory Upert,Nicolas Smargiasso,Nicolas Gilles,Loïc Quinton,Edwin De Pauw
标识
DOI:10.1021/acs.analchem.5b00245
摘要
Disulfide bonds are post-translational modifications (PTMs) often found in peptides and proteins. They increase their stability toward enzymatic degradations and provide the structure and (consequently) the activity of such folded proteins. The characterization of disulfide patterns, i.e., the cysteine connectivity, is crucial to achieve a global picture of the active conformation of the protein of interest. Electron-transfer dissociation (ETD) constitutes a valuable tool to cleave the disulfide bonds in the gas phase, avoiding chemical reduction/alkylation in solution. To characterize the cysteine pairing, the present work proposes (i) to reduce by ETD one of the two disulfide bridges of model peptides, resulting in the opening of the cyclic structures, (ii) to separate the generated species by ion mobility, and (iii) to characterize the species using collision-induced dissociation (CID). Results of this strategy applied to several peptides show different behaviors depending on the connectivity. The loss of SH· radical species, observed for all the peptides, confirms the cleavage of the disulfides during the ETD process.
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