Unexpected Research Results in a Biochemistry Laboratory Course Lead to New Avenues for Social Justice in Education
By: Danny Mendoza, Kristian Culla, Lubat Asadova, Helena Dommer
Department: Biology, Chemistry & Biochemistry
Faculty Advisor: Dr. Misty Kuhn
The genesis of this research project was from a CHEM 343 biochemistry I laboratory. The final for the class called for the lab groups to choose different types of chromatography to purify watermelon glyoxylate malate dehydrogenase (wg-MDH) protein. This method was selected to give students experience working with an FPLC instrument and to learn how to read and interpret chromatograms. The results from these experiments became the motivation of our current research because of how remarkably well-defined its corresponding SDS-PAGE turned out. It was especially outstanding since these results implied that there was even greater specificity in protein purification when using a cation exchange column instead of the well-established, high specificity of the nickel-affinity column that had been used previously by students in the CHEM 343 laboratory. During this experience, the class became invested in understanding the possible applications of using cation exchange columns over nickel affinity to take advantage of its benefits like cheaper cost, less toxic waste, and possibly having a wider range of proteins that could be purified when nickel-affinity chromatography failed. To test the viability of cation-exchange chromatography for various proteins, we repeated our experiments with the wg-MDH protein to ensure reproducibility. Furthermore, we tested this approach with other unrelated proteins with different functions that have different pIs, molecular weights, and structures.