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