Barrett, The Honors College Thesis/Creative Project Collection
Barrett, The Honors College at Arizona State University proudly showcases the work of undergraduate honors students by sharing this collection exclusively with the ASU community.
Barrett accepts high performing, academically engaged undergraduate students and works with them in collaboration with all of the other academic units at Arizona State University. All Barrett students complete a thesis or creative project which is an opportunity to explore an intellectual interest and produce an original piece of scholarly research. The thesis or creative project is supervised and defended in front of a faculty committee. Students are able to engage with professors who are nationally recognized in their fields and committed to working with honors students. Completing a Barrett thesis or creative project is an opportunity for undergraduate honors students to contribute to the ASU academic community in a meaningful way.
As prices for fuel along with the demand for renewable resources grow, it becomes of paramount importance to develop new ways of obtaining the energy needed to carry out the tasks we face daily. Costs of production due to energy and time constraints impose severe limitations on what is viable.…
As prices for fuel along with the demand for renewable resources grow, it becomes of paramount importance to develop new ways of obtaining the energy needed to carry out the tasks we face daily. Costs of production due to energy and time constraints impose severe limitations on what is viable. Biological systems, on the other hand, are innately efficient both in terms of time and energy by handling tasks at the molecular level. Utilizing this efficiency is at the core of this research. Proper manipulation of even common proteins can render complexes functionalized for specific tasks. In this case, the coupling of a rhenium-based organometallic ligand to a modified myoglobin containing a zinc porphyrin, allow for efficient reduction of carbon dioxide, resulting in energy that can be harnessed and byproducts which can be used for further processing. Additionally, a rhenium based ligand functionalized via biotin is tested in conjunction with streptavidin and ruthenium-bipyridine.
Over the past two decades, a significant amount of research has been conducted investigating cyanovirin-N (CVN), which has been shown to be an effective antiviral agent by inhibiting entry of HIV into the cell. The virucidal activity of CVN is attributed to the tight binding interactions with the glycosylated surfaces…
Over the past two decades, a significant amount of research has been conducted investigating cyanovirin-N (CVN), which has been shown to be an effective antiviral agent by inhibiting entry of HIV into the cell. The virucidal activity of CVN is attributed to the tight binding interactions with the glycosylated surfaces of the envelope protein gp120. In this study we investigated how the incorporation of various single point mutations in the glycan binding site would ultimately affect the overall binding affinity of the protein with the glycan. These mutations were predicted through computational methods. Using a BP-docking program and molecular dynamics (MD) simulation, the free energy change upon the ligand binding to the each protein was determined. Experimental work and Isothermal Titration Calorimetry (ITC) was used to determine the Kd values for each protein mutant. A total of three different CVN mutants, T57S, S52T, and a double mutant T57S-S52T, or simply TS, were investigated on the background of P51G-m4-CVN. After conducting the experimental work, it was concluded that the overall fold and stability of the protein was conserved for each mutant. ITC data showed that T57S displayed the lowest dissociation constant valued in the micromolar range. In fact, T57S had a much lower Kd value in comparison to P51G-m4. In contrast, the double mutant TS, showed poor binding affinity for the glycan. When comparing experimental data with the data provided by MD simulation and BP-docking, the results were fairly correlated for all mutants, except for that of the double mutant, TS. According to information provided by MD simulation and BP docking, the binding of the sugar to TS is a very exergonic reaction, which is indicative of very negative free energy change (ΔG). However, the experimental Kd, which was very high, contradicts this data and is thus indicative of lower binding affinity for the glycan. This contradiction is currently being investigated.
