Observation of Water Molecules Bound to a Protein Using Cold-Spray Ionization Mass Spectrometry
Observation of Water Molecules Bound to a Protein Using Cold-Spray Ionization Mass Spectrometry
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DOI：
10.2116/analsci.21.449
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发表时间：
2005-04
影响因子：
1.6
通讯作者：
Y. Sei;S. Shimotakahara;J. Ishii;H. Shindo;H. Seki;K. Yamaguchi;M. Tashiro
中科院分区：
文献类型：
--
作者：
Y. Sei;S. Shimotakahara;J. Ishii;H. Shindo;H. Seki;K. Yamaguchi;M. Tashiro
用冷喷雾电离质谱（CSI-MS）对核糖核酸酶T_1（RNase T_1）结合的水分子进行了表征。CSI-MS是电喷雾电离质谱（ESI-MS）在低温下操作的变体，并且特别适合于研究较弱的分子缔合，因为喷雾界面处的温度远低于常规ESI-MS中的温度。在这种方法中，在48°C的喷雾温度下鉴定了由于添加9个水分子而产生的离子峰。这一结果与NMR和X射线晶体学的组合分析所推断的结果显示出良好的一致性，表明CSI-MS能够快速提供可靠的信息来表征结合到大分子上的水分子的数量。
The characterization of water molecules bound to ribonuclease T_1 (RNase T_1) was carried out using cold-spray ionization mass spectrometry (CSI-MS). CSI-MS is a variant of electrospray ionization mass spectrometry (ESI-MS) operating at low temperature, and is particularly suitable for investigating the weaker molecular associations, since the temperature at the spray interface is much lower than that in the conventional ESI-MS. In this approach, ion peaks due to the addition of nine water molecules were identified at a spray temperature of 48°C. This result showed good agreement with that inferred by the combinational analysis of NMR and X-ray crystallography, indicating that CSI-MS is capable of rapidly providing reliable information to characterize the number of water molecules bound to a macromolecule.