This award is supported by the Major Research Instrumentation and the Chemistry Research Instrumentation Programs. Professor Laura Hawk from Grand Valley State University and colleagues Shannon Biros, Andrew Lantz, Paul Cook and Dalila Kovacs are acquiring a compact a liquid-chromatograph mass-spectrometer (LCMS) having a single quadrupole mass analyzer. The mass spectrometer is equipped with a series of ionization sources such as electrospray ionization (ESI), an atmospheric pressure chemical ionization/atmospheric solid analysis probe (APCI/ASAP), as well as a thin layer chromatography (TLC) plate reader. 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 samples. In a typical experiment, the components are heated and flow into a mass spectrometer where they are ionized. The ions' masses are measured very accurately. This highly sensitive technique allows the structure of molecules in complex mixtures to be studied. An instrument with a liquid chromatograph can separate mixtures of compounds before they reach the mass spectrometer. The various ionization sources provide added flexibility with regard to the types of samples that are analyzed. The acquisition strengthens the research infrastructure at the University and regional area. The instrument broadens participation by involving diverse groups of students in research and research training using this modern analytical technique. This instrument acquisition supports many female and underrepresented investigators. It also provides training opportunities to undergraduate students, many of whom are first-generation students. The instrument gives students experience using vital instrumentation that they carry with them into their careers.
The award of this mass spectrometer is aimed at enhancing research and education at all levels. It especially impacts studies of beneficial amyloids which are aggregates of proteins that become folded into various shapes. The instrument is used to evaluate the role of intrinsically-disordered regions in protein structure and function as well as the development of ligands for the separation of critical elements such as rare earth (f) elements. The mass spectrometer is employed in studies of enzymes that inactivate antibiotics in bacteria and for the development of organic flow cell electrolytes for batteries. The instrument also serves researchers investigating the conversion of biomass into commodity chemicals and those looking for targets of the protein focal adhesion kinase.
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.
