Collaboration in Chemistry

Zach Strickland ’21, Motley, Minn.
Majors/Minors: Neuroscience, Biology; Chemistry, Religion

Please tell us about your experience in researching enzymes.

I worked in the chemistry department last summer with Dr. David Mork. Our research project focused on understanding the mechanism of glutamate dehydrogenase, an enzyme active in cellular metabolism, using product inhibition studies. Because one of the products of glutamate dehydrogenase absorbs light at 340 nanometers, we were able to track the speed at which the enzyme works under different conditions over time. By analyzing how exposure to the products of the overall reaction affects the enzyme, we were able to establish patterns of inhibition for the enzyme. Then, by comparing these inhibition patterns, we could establish a highly likely binding order for substrates and release order for products. Sadly, since we can’t literally visualize the different transition states in the enzyme, we can’t ever “prove” a mechanism is true.

How did you learn about this research opportunity?

I knew that I wanted to spend my summer doing scientific research, so I looked for interesting opportunities on campus. Both the biology and chemistry departments offer paid summer research internships through the office of undergraduate research, so I applied through the chemistry department. Summer research is open to students of all academic disciplines and is something I would highly recommend.

What about this area of study interests you?

Some scientists divide biology into two “camps” – one that focuses on the larger organismal and ecological levels of organization and one that focuses on the world of and within the cell. I love small-scale biology. I’m fascinated by the things that we can’t easily visualize without a microscope but can still evaluate using instruments and lab techniques. Additionally, enzymes are fascinating because they make reactions that wouldn’t normally happen work much more effectively and are present in virtually every living organism.

How was working in the Integrated Science Center for your research?

The ISC is an amazing place to work. It’s both beautiful and functional. From my lab bench, I can see all the way to Olin Hill and 8th Street. It’s wonderful to be able to see the campus from the lab. Also, the ISC was designed for collaboration. I love walking around and looking in on other labs and classrooms and seeing those scientists hard at work. It’s very common for us to come in and see what the other is working on. Most importantly, everything I need for my research – from cell culture to spectrophotometry instruments – are easily accessible either in my lab or nearby. There’s no walking to the other side of campus for materials or reagents.

How was your research collaboration?

I worked with Dr. David Mork, an enzyme biochemist in the chemistry department. I really enjoyed his mentorship and learned a great deal not only about biochemistry and lab techniques but about how to let your results guide your next steps and to design new experiments.

What skills did the research help you gain or discover?

I gained a wide variety of technical skills in the biochemistry realm. Because I was the only research student working on this project, I got to learn how to do everything that the project needed to be successful. Because we started the summer by growing up a strain of E. coli that expressed our enzyme, isolated the enzyme from the E. coli, and then did our experiments on the enzyme, I not only learned about how to measure enzyme kinetics but the background skills in media preparation, cell culture, and enzyme purification. Unlike a lab experiment for a course where you have a protocol and you know what your data should say at the end, we didn’t know what the end result “should” be. This taught me to let my findings inform the next steps of my research, an essential skill for a scientist.

What was the highlight of your research?

About six weeks into the project, we realized that the data I’d collected was beginning to tell a coherent story for our enzyme and point toward a highly ordered mechanism. A few experiments later, we discovered that all of the data pointed toward the same conclusion about the mechanistic order for EcGDH.

What is the biggest takeaway from your time conducting research?

This project allowed me to experience the excitement of designing my own experiments, collaborating with other scientists, and seeing my work get results. I think my biggest takeaway was realizing that scientific research is something that I see myself doing for my career.

^{Published May 2020}