Motolani Matthew, a graduate student in the Department of Chemistry and Biochemistry and a research student at the Arkansas Statewide Mass Spectrometry Facility, under the guidance of professor Jackson O. Lay Jr., has been accepted to participate in the 2023 Clinical and Translational Research Summer course hosted by the National Institutes of Health.

This course aims to showcase the contributions of Ph.D. scientists in the field of clinical and translational research. It provides a comprehensive overview and practical examples of how fundamental scientific knowledge and clinical observations converge to drive translational research. Furthermore, it aims to enhance awareness and accessibility to Ph.D. role models and potential career opportunities at the NIH.

The NIH Summer Course, organized by the NIH Office of Clinical Research Education and Collaboration Outreach in Bethesda, Maryland, is an immersive introductory program. It is designed for graduate students pursuing a Ph.D. in the basic sciences at a U.S. institution or those involved in the NIH Graduate Partnership Program. Originally launched as a course for basic science graduates, the course has expanded its reach since 2019 to accommodate a wider range of participants. Enrollment eligibility requires completion of at least one year of doctoral study by July 2023 and throughout July 2023. Prospective students must be actively pursuing their first doctoral degree and possess the approval of their dean or research adviser to take part in the course. The course is open to a maximum of 30 students this year and is scheduled to be held from July 17-21.

Matthew's research focuses on the elucidation of protein stability and structural information using hydrogen-deuterium exchange mass spectrometry techniques. Specifically, she has optimized the Protein Equilibrium Population Snapshot hydrogen-deuterium exchange electrospray ionization mass spectrometry (PEPS) method. This method is used for protein equilibrium unfolding measurements and allows for the determination of stability parameters for both intact proteins and peptic fragments. PEPS offers the advantage of mitigating user bias by utilizing a nonlinear model fitting tool of the calculated molecular weight unfolding curve to the experimental molecular weight curve.  Motolani Matthew has applied the PEPS method to study staphylococcal nuclease and human acidic fibroblast growth factor 1 (hFGF1) wildtype and mutants.

Additionally, Matthew is actively working on expanding the application of the PEPS method to characterize more mutants of hFGF1. This involves studying the folding and unfolding rates of these mutants, providing insights into their structural dynamics and stability. Being a research student at the Arkansas Statewide Mass Spectrometry Facility, she has a unique opportunity and has acquired expertise in the diverse range of mass spectrometry techniques offered by the facility, such as GC-MS, HPLC-ESI-MS, and MALDI-TOF.