Student Spotlight: Lucian Murray

This summer undergraduate student Lucian Murray was awarded funds from Appalachian’s Research Institute for Environment, Energy, and Economics (RIEEE) for his research with Dr. Hester. His research seeks to develop a synthetic chemical to combat warming trends in the atmosphere. Lucian is conducting his research in the Biophysics and Optical Sciences Facility (BiyOSeF) in Garwood. To read more about Lucian's research and the work conducted in the BiyOSeF facility, read below.

The chemical dimethyl sulfide (DMS) plays an important role in the sulfur cycle within Earth’s atmosphere. The degradation of DMS produces sulfur dioxide (SO2) molecules that attract surrounding water molecules, which results in increased cloud condensation nuclei (CCN) and increased Earth albedo. Thus, we hope to develop a way to create synthetic DMS to combat warming trends in the stratosphere. It is theorized that the enzyme DMS monooxygenase is responsible for DMS degradation. The enzyme DMS monooxygenase works through two subunits, DmoA and DmoB; two proteins that have not been fully characterized. To identify the two subunits responsible for DMS degradation, we study candidate proteins that are believed to be the true DmoA and DmoB subunits. We use two techniques known as fluorescence spectroscopy and fluorescence anisotropy to determine if the candidate proteins are the true subunits in DMS monooxygenase. 

The Biophysics and Optical Sciences Facility (BiyOSeF) houses a custom-built fluorescence instrument. In fluorescence, the sample is excited with a narrow range of light wavelengths. We have coupled our fluorescence instrument to a high-resolution low-noise spectrometer to ensure that detected light is within the desired wavelength range instead of excitation light or other unwanted radiation. Using this instrument, we measure fluorescence intensity of only the desired wavelength range. We mix fluorescent flavin mononucleotide (FMN) with the candidate proteins for DmoA and DmoB, and when they bind, the FMN fluorescence is expected to increase or decrease depending on the protein. Fluorescence intensities at varying concentrations of FMN and DmoA or DmoB and the resulting fluorescence intensity levels are measured and analyzed to determine if binding has occurred. This technique can be used to study, among other things, whether or not the binding of a fluorescent molecule to a large protein occurs. 

This research is a joint project between the Appalachian State University Department of Chemistry and the Appalachian State University Department of Physics and Astronomy. The project is funded by Appalachian’s Research Institute for Environment, Energy, and Economics (RIEEE). Appalachian’s RIEEE decided to fund our project as its goals and motivations involve the intersections of environment, energy, and economics.

Published: Sep 9, 2019 11:48am