A New Cryo-Ion Mobility Spectrometer for Studies of Biomolecule Hydration

在化学系化学测量和成像计划的支持下，德克萨斯农工大学的大卫·拉塞尔教授正在开发一种新的仪器，用于研究被几个水分子包围的带电物种。正在开发的仪器被称为冷冻离子迁移率质谱仪(c-IM-MS)，它可以通过监测电荷在极低温度下在长管中飞行的方式来确定电荷物种的大小和结构。罗素教授的研究提供了帮助理解水分子在影响蛋白质结构和功能中的作用的信息，特别是那些与蛋白质直接接触的分子。所获得的知识最终将使人们能够更好地理解许多重要的生物和化学问题，例如抗冻蛋白如何保护生活在寒冷气候中的植物和鱼类。从事这个项目的学生有机会获得仪器制造和生物分子研究的经验。该仪器的设计将与该领域的其他科学家共享，因此将开发的方法可以广泛用于回答关于蛋白质和其他生物分子在水中如何行为的结构性问题。在过去的十年中，罗素实验室开发了几个c-IM-MS仪器原型，并描述了展示c-IM-MS仪器无与伦比能力的概念验证研究。实验观察作为水合程度函数的结构变化的能力对于建立结构/功能关系至关重要。这些研究补充了生物分子结构/功能关系计算研究的快速增长-在理论和实验结果之间得出相关性的能力。在这个项目中，罗素教授专注于下一代仪器的设计，他结合了一些最新的技术创新，包括对更大的蛋白质和蛋白质复合体的研究。他从离子透过率和对离子脱水的影响以及与现有MS分析仪对比的基准仪器性能方面对仪器的整体性能进行了评估。最终目标是开发一种能够更好地理解多肽-水相互作用并回答诸如水化如何影响多肽构象偏好以及多肽如何改变水结构等问题的仪器。

With support from the Chemical Measurement and Imaging Program in the Division of Chemistry, Professor David Russell at Texas A&M University is developing a novel instrument to study charged species surrounded by a few water molecules. The instrument being developed is called cryo-ion mobility-mass spectrometer (c-IM-MS) and it can determine the size and structure of the charge species by monitoring how they fly in a long tube under an extreme low temperature. Professor Russell's study are providing information to help understand the role of water molecules in affecting protein structure and function, especially those in direct contact with proteins. The gained knowledge will ultimately enable better understanding of many important biological and chemical questions, such as how antifreeze proteins protect plants and fish living in cold climates. The students working on this project have the opportunity to gain experience for both instrument building and biomolecule studies. The instrument design will be shared with other scientists in the field so the to-be-developed approach can be widely used to answer structural questions about how proteins and other biomolecules behave in water.During the past decade, the Russell laboratory has developed several prototype c-IM-MS instruments and described proof-of-concept studies that illustrate the unparalleled capabilities of the c-IM-MS instrument. The ability to experimentally observe structural changes that are a function of the extent of hydration is critical for establishing structure/function relationships. Such studies compliment the rapid growth in computational studies of biomolecule structure/function relationships---the ability to draw correlations between theoretical and experimental results. In this project, Professor Russell focuses on the design of the next-generation instrument by incorporating a number of recent technological innovations to include studies of larger proteins and protein complexes. He evaluates the overall instrument performance in terms of ion transmission and effects on ion dehydration and benchmark instrument performance against existing MS analyzers. The ultimate goals are to develop an instrument that is capable of better understanding peptide-water interactions and answering questions such as how does hydration affect peptide conformational preferences, and how does the peptide alter the structure of water.