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首页> 外文期刊>Journal of mass spectrometry: JMS >In ESI-source H/D exchange under atmospheric pressure for peptides and proteins of different molecular weights from 1 to 66kDa: the role of the temperature of the desolvating capillary on H/D exchange
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In ESI-source H/D exchange under atmospheric pressure for peptides and proteins of different molecular weights from 1 to 66kDa: the role of the temperature of the desolvating capillary on H/D exchange

机译：在常压下ESI源H / D交换中，分子量为1至66kDa的不同分子量的肽和蛋白质：去溶剂化毛细管的温度对H / D交换的作用

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Transition of proteins from the solution to the gas phase during electrospray ionization remains a challenging problem despite the large amount of attention it has received during the past few decades. One of the major questions relates to the extent to which proteins in the gas phase retain their condensed phase structures. We have used in-electrospray source hydrogen/deuterium exchange to determine the number of deuterium incorporations as a function of protein mass, charge state and temperature of the desolvating capillary where the reaction occurs. All experiments were performed on a Thermo LTQ FT Ultra equipped with a 7-T superconducting magnet. Ions were generated by an IonMax Electrospray ion source operated in the positive ESI mode. Deuterium exchange was performed by introducing a droplet of D2O beneath the ESI capillary. We systematically investigated gas phase hydrogen/deuterium (H/D) exchange under atmospheric pressure for peptides and proteins of different molecular weights from 1 to 66kDa. We observed that almost all proteins demonstrate similar exchange rates for all charge states and that these rates increase exponentially with the temperature of the desolvating capillary. We did not observe any clear correlation of the number of H/D exchanges with the value of the cross section for a corresponding charge state. We have demonstrated the possibility of performing in-ESI source H/D exchange of large proteins under atmospheric pressure. The simplicity of the experimental setup makes it a useful experimental technique that can be applied for the investigation of gas phase conformations of proteins. Copyright (c) 2015 John Wiley & Sons, Ltd.
机译：尽管在过去几十年中受到了广泛的关注，但在电喷雾电离过程中蛋白质从溶液到气相的转变仍然是一个具有挑战性的问题。主要问题之一涉及气相中的蛋白质在多大程度上保持其冷凝相结构。我们已经使用电喷雾源氢气/氘交换来确定氘结合的数量，该数量是蛋白质质量，荷电状态和发生反应的去溶剂化毛细管的温度的函数。所有实验均在配备7-T超导磁体的Thermo LTQ FT Ultra上进行。离子由在正ESI模式下运行的IonMax电喷雾离子源产生。通过在ESI毛细管下方引入D2O液滴来进行氘交换。我们系统地研究了在大气压下气相氢/氘（H / D）交换不同分子量从1至66kDa的肽和蛋白质的过程。我们观察到，几乎所有蛋白质对于所有电荷状态都表现出相似的交换速率，并且这些速率随着去溶剂化毛细管的温度呈指数增加。我们没有观察到H / D交换次数与相应电荷状态的横截面值有任何明显的相关性。我们已经证明了在大气压下进行大蛋白的ESI源H / D交换的可能性。实验装置的简单性使其成为一种有用的实验技术，可用于研究蛋白质的气相构象。版权所有（c）2015 John Wiley＆Sons，Ltd.

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