MRI: Acquisition of a High Resolution, Quadrupole Mass Spectrometer to Enable Research and Education at the Interface of Chemistry and Biology

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This award is supported by the Major Research Instrumentation and the Chemistry Research Instrumentation programs. Professor Ken Shimizu from University of South Carolina Columbia and colleagues Qian Wang, Michael Walla, Thomas Makris and Norma Frizzell have acquired a high-resolution quadrupole time-of-flight mass spectrometer (HR-Q-ToF-MS) equipped with a series of attachments. In general, mass spectrometry (MS) is one of the key analytical methods used to identify and characterize small quantities of chemical species embedded in complex matrices. In a typical experiment, the components flow into a mass spectrometer where they are ionized into the parent ion and its fragment ions and their masses are measured. This highly sensitive technique allows detection and determination of the structure of molecules in a complex mixture. An instrument with a liquid chromatograph provides additional structural identification power by separating mixtures of compounds before they reach the mass spectrometer. In a quadrupole mass analyzer, there are four cylindrical rods parallel to each other which are responsible for filtering sample ions, based on their mass-to-charge ratio (m/z). Ions are separated based on the stability of their trajectories in the oscillating electric fields applied to the rods. The acquisition strengthens the research infrastructure at the University and regional area. The instrument broadens participation by involving diverse students in research and research training using this modern analytical technique. It provides training opportunities to faculty and students from neighboring Historically Black College Universities (HBCUs) such as Benedict College, South Carolina State University, and Claflin University. The instrument supports partnerships with many local companies and government agencies.The proposal is aimed at enhancing research and education at all levels. It is especially useful for the characterization of compounds obtained by selectively functionalizing carbon-hydrogen bonds of natural products, and for exploring protein assembly, bioconjugation chemistry, and biomaterials sciences. The instrument is essential for studying protein succination and non-enzymatic chemical modification of protein thiol residues, and for studying the impacts of wastewater reuse, hydraulic fracturing, and coal-fired power plant discharges on drinking water. The mass spectrometer is used for the identification of mechanisms needed to maintain adequate intracellular levels of the essential metal iron and mitochondrial control of thiol-disulfide redox balance. The instrument is also used to determine plants response to environmental stress, for understanding connections amongst neurons, and deciphering the molecular pathways regulating cytoplasmic dynein, a cytoskeletal motor protein that move along microtubules in cells.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.