MRI: Acquisition of a Hybrid Supercritical Chromatography, High-Pressure Chromatograph, Quadrupole-Time-of-Flight Mass Spectrometer (SFC/UHPLC Q-ToF/MS)

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This award is supported by the Major Research Instrumentation and the Chemistry Research Instrumentation programs. Professor Joseph Genereux from University of California Riverside and colleague Ming Tang have acquired a hybrid supercritical chromatography, ultrahigh pressure liquid chromatograph, quadrupole time-of-flight mass spectrometer (SFC/UHPLC Q-ToF/MS). In general, mass spectrometry (MS) is one of the key analytical methods used to identify and characterize small quantities of chemical species in complex matrices. In a typical experiment, the components flow into a mass spectrometer where they are ionized and the ion masses are measured. This highly sensitive technique allows detection and determination of the structure of molecules in a complex mixture. An instrument with a supercritical chromatograph provides additional structural identification power by separating mixtures of compounds using high pressures and temperature before they reach the mass spectrometer. In the ToF method the mass-to-charge ratio of an ion is determined by the way of a time measurement in which ions are accelerated by an electric field of known strength. 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. The instrument serves as a tool for broadening the participation of women and underrepresented minorities in science and engineering research at this Hispanic Serving Institution.The award of this unique mass spectrometer is aimed at enhancing research and education at all levels. It especially allows the use of electrophilic foot printing to identify protein conformational changes in complex media and the creation of branched dendrimeric architectures for energy transmission. The mass spectrometer aids the characterization of non-covalent interactions between proteins and structured or modified nucleic acids and the identification of aspartic acid epimerization in the aging proteome. The instrument is also used to study self-sorting, supramolecular catalysis and molecular dynamics as well as to investigate serine peptide assembly. The mass spectrometer also serves researchers studying structure and mechanism in tryptophan synthase and exploring olefin polymerization catalysts with ligands featuring weakly coordinating carborane anions. The instrumentation is also used in analyzing protein biogenesis and protein quality, using metabolomics for deciphering t-cell heterogeneity and using asymmetric methods and synthesis strategies for the study of neuroprotective limonoids. It is also employed to study effects of post-transcriptional and post-translational modifications on the dynamics of eukaryotic translation initiation and to obtain entioselectivity from gold(III) complexes.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.