Effects of select anions from the Hofmeister series on the gas-phase conformations of protein ions measured with traveling-wave ion mobility spectrometry/mass spectrometry.
Effects of select anions from the Hofmeister series on the gas-phase conformations of protein ions measured with traveling-wave ion mobility spectrometry/mass spectrometry.
复制标题
使用行波离子迁移谱/质谱法测量霍夫迈斯特系列中的精选阴离子对蛋白质离子气相构象的影响。
DOI：
10.1007/s13361-011-0238-1
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发表时间：
2011-11
影响因子：
3.2
通讯作者：
Williams, Evan R.
中科院分区：
文献类型：
--
作者：
Merenbloom, Samuel I.;Flick, Tawnya G.;Daly, Michael P.;Williams, Evan R.
通过电喷雾电离（ESI）从含有5 mM高氯酸铵、碘化铵、硫酸铵、氯化铵、硫氰酸铵或氯化胍的水溶液中形成的泛素、细胞色素c、溶菌酶和α-乳白蛋白离子的气相构象，使用与飞行时间（TOF）质谱（MS）耦合的行波离子迁移谱（TWIMS）进行检查。对于泛素、细胞色素c和β-乳白蛋白，多个酸分子的加合导致从水溶液形成的最高和最低电荷状态没有显著的构象变化，而中间电荷状态变得更紧凑。过渡到更紧凑的构象的中间电荷状态发生较少的绑定H2SO 4分子比HClO 4或HI分子，这表明离子-离子或盐桥相互作用稳定更紧凑的形式的气态蛋白质。然而，漂移时间分布的蛋白质离子相同的净电荷与最高水平的加合的每种酸是可比的，这表明这些蛋白质离子都采用类似的紧凑的构象或家庭的构象。当多个酸分子加合到溶菌酶的电荷状态时，没有观察到构象的变化。这些结果表明，HClO 4，HI，或H2SO 4的连接到多质子化的蛋白质可以诱导在所得的气相蛋白质离子的紧凑的构象。相反，不同的霍夫迈斯特效应观察到相应的阴离子在溶液中在较高的浓度。
The gas-phase conformations of ubiquitin, cytochrome c, lysozyme, and ↦-lactalbumin ions, formed by electrospray ionization (ESI) from aqueous solutions containing 5 mM ammonium perchlorate, ammonium iodide, ammonium sulfate, ammonium chloride, ammonium thiocyanate, or guanidinium chloride, are examined using traveling-wave ion mobility spectrometry (TWIMS) coupled to time-of-flight (TOF) mass spectrometry (MS). For ubiquitin, cytochrome c, and ↦-lactalbumin, adduction of multiple acid molecules results in no significant conformational changes to the highest and lowest charge states formed from aqueous solutions, whereas the intermediate charge states become more compact. The transition to more compact conformers for the intermediate charge states occurs with fewer bound H2SO4 molecules than HClO4 or HI molecules, suggesting ion-ion or salt-bridge interactions are stabilizing more compact forms of the gaseous protein. However, the drift time distributions for protein ions of the same net charge with the highest levels of adduction of each acid are comparable, indicating that these protein ions all adopt similarly compact conformations or families of conformers. No change in conformation is observed upon the adduction of multiple acid molecules to charge states of lysozyme. These results show that the attachment of HClO4, HI, or H2SO4 to multiply protonated proteins can induce compact conformations in the resulting gas-phase protein ions. In contrast, differing Hofmeister effects are observed for the corresponding anions in solution at higher concentrations.
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DOI：
10.1073/pnas.93.7.3143
发表时间：
1996-04-02
影响因子：
11.1
作者：
Gross, DS;Schnier, PD;Williams, ER
通讯作者：
Williams, ER
DOI：
10.1039/ft9938901215
发表时间：
1993-04-21
期刊：
JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS
影响因子：
--
作者：
HOLZ, M;GRUNDER, R;MELELEO, A
通讯作者：
MELELEO, A
影响因子：
7.4
作者：
Badman, ER;Hoaglund-Hyzer, CS;Clemmer, DE
通讯作者：
Clemmer, DE
影响因子：
2.9
作者：
HARDING, MM;WILLIAMS, DH;WOOLFSON, DN
通讯作者：
WOOLFSON, DN
影响因子：
1.8
作者：
Freitas, MA;Hendrickson, CL;Marshall, AG
通讯作者：
Marshall, AG