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Dr. Beth Stroupe is a Professor in the Department of Biological Science and the Institute of Molecular Biophysics at Florida State University (FSU). She is also Director of the Molecular Biophysics Graduate Program there. Beth completed her undergraduate training at Wake Forest University where she majored in chemistry and minored in music. She was awarded her PhD in biochemistry from the Scripps Research Institute. Afterwards, Beth conducted postdoctoral research at Brandeis University before joining the faculty at FSU where she is today. In our interview, Beth shares more about her life and science.
People Behind the Science Podcast Show Notes
Life Outside of Science (2:44)
When she’s not working, Beth and her partner enjoy spending quality time with their two cats, as well as growing black-eyed peas and other vegetables in their garden, kayaking, hiking, and exploring the great outdoors.
The Scientific Side (4:07)
Research in Beth’s lab focuses on understanding what molecules and proteins look like. This is important for better understanding how these molecules work, both from a basic science perspective and with an eye towards controlling molecules for clinical applications. They use a variety of different techniques that allow them to visualize these very tiny molecules.
A Dose of Motivation (6:34)
“It is said sometimes that the great teachers and mentors, the rabbis and gurus, achieve their ends by inducting the disciple into a kind of secret circle of knowledge and belief, make of their charisma a kind of gift… I suspect that the best teachers… do something else. They don’t mystify the work… but insist that all the magic they have to offer is a commitment to repetition and perseverance. The great oracles may enthrall, but the really great teachers demystify.” – Adam Gopnik
What Got You Hooked on Science? (10:21)
Beth likes to joke that a Mendelian genetic cross between her mom, who was a mathematician and statistician, and her dad, who was an analytical biochemist, was bound to result in her becoming a structural biologist because structural biologists use biochemistry and mathematics to understand what molecules look like. As an undergraduate student, Beth took inorganic chemistry and biochemistry at the same time. In doing so, she was struck by the idea that everything on Earth comes from interactions between the sun and the metal-containing molecule chlorophyl, which turns sunlight into energy. Following her interests, Beth discovered the field of metalloenzyme chemistry, which focuses on the biological chemistry performed by enzymes that use metal ions to enhance their chemicals. She was hooked. Throughout her training, Beth focused on learning and applying the latest structural biology techniques to better understand metalloenzymes, and she continues to work in this area today.
The Low Points: Failures and Challenges (18:12, 23:50)
Since graduate school, Beth has been interested in preserving and visualizing an enzyme called sulfite reductase. The enzyme has two different protein components that come together to reduce sulfur from sulfite into sulfide. When she first started working on the project, it was really difficult to make the enzyme, and cryogenic electron microscopy technology wasn’t as advanced as it is now. The lab had just solved the structure of one of the protein subunits, and Beth planned to determine how that subunit interacted with the other subunit to perform the really cool chemistry involved in creating sulfide. Despite her best efforts, she failed.
Over the next 30 years, technology and biochemistry have advanced to the point where it became possible to determine the structure of just those two subunits interacting. This has allowed the field to understand the basic assembly unit for the larger complex. The next big step is to determine the structure of the whole enzyme which is made of 12 subunits (8 copies of one subunit and 4 copies of the other subunit). Unfortunately, to be able to visualize the whole enzyme, they need all the pieces to be properly aligned and very still. This has been particularly challenging, and almost everyone who has passed through her lab has tried to make progress on this project. They’ve been incrementally overcoming obstacles, but it has taken a long time and a lot of effort from many individuals. Despite the setbacks, Beth is optimistic that they will be successful soon!
A Shining Success! (27:51)
Solving the structure of the interaction between the two subunits was a big success in the quest to visualize the whole sulfite reductase enzyme. When she launched her independent research laboratory, one of Beth’s major goals was to disprove a hypothesis from the 1970s that there were these 12 subunits bound together with 8 copies of one subunit and 4 copies of the other subunit. However, none of their research to date has been able to disprove this hypothesis. Beth began to suspect that maybe the old hypothesis was correct. She shifted her efforts to trying to discover what the structure looked like, but nothing they did worked. Pivoting again, Beth began collaborating with the National High Magnetic Field Laboratory at FSU to use a different approach, which revealed that the two subunits interacted in a really unexpected way. It was so exciting when they were finally able to use cryogenic electron microscopy to solve the structure and see the detailed atomic-resolution basis for the unusual interaction between the subunits. The lab celebrated by going out to dinner, and they brought their lab mascot Henry Sparkles to the party as well.
Book Recommendations (32:16)
The Heart Is a Lonely Hunter by Carson McCullers
Most Treasured Travel (33:14)
One of Beth’s first international collaborations was with a group in the United Kingdom (UK), and she still cherishes her time spent there as a graduate student. The lab members were incredibly welcoming and taught her a lot. This was her first time working in a lab outside of the United States, and it was cool to be surrounded by individuals from many different countries and cultures. If you’re able to visit, Beth highly recommends visiting Wales and hiking in the Lake District in northern England. Over the years, Beth has continued to stay in touch with people she met in the UK, and they have fun catching up at conferences.
Quirky Traditions and Fond Memories (36:22)
Beth was lucky to have met Dr. Don Caspar, a pioneer in the field who originally coined the term “structural biology” to describe what was (at the time) a new approach to understanding how biology works on a molecular level. Don worked with Rosalind Franklin at King’s College London in the mid 1950’s when she and colleagues were trying to solve the structure of DNA, and he had so many wonderful stories to share about his life and career. Before joining the faculty at FSU, Don worked at Brandeis, and Beth’s positions at both institutions overlapped with his time there. Rather than being an imposing or intimidating figure like you might imagine, Don was incredibly kind and a steadfast supporter of trainees and women in science. He loved structural biology so much that he wanted to share it with everyone he met and trained.
Advice For Us All (40:37)
Don’t let other people bring you down. Give yourself a day to be upset or disappointed when you get negative feedback, but then get back up and move on. Being an academic scientist is difficult, but very important. Just keep moving forward.
Guest Bio
Beth’s research is aimed at understanding what proteins look like to understand how they work. Her lab’s primary target is a multi-component metalloenzyme called sulfite reductase that contains four copies of an iron-containing enzyme and eight copies of a flavin-binding reductase. Although sulfite reductase has been studied in depth since the 1960s and 70s, we still do not know how the 12 subunits assemble to make the active holoenzyme or how the subunits interact enzymatically. After decades of failure, her lab recently determined a minimal complex to show how two of the 12 subunits interact structurally, but the interaction is not what one might predict. Now, her lab is setting out to overcome the technical challenges of structural studies on a mobile biomolecular machine that catalyzes essential chemistry for life. This work is important because humans cannot effectively replicate the chemistry performed by sulfite reductase – a six-electron reduction of sulfite to sulfide. In fact, when you hear about nitrogen fertilizer plants catching on fire, it is because the analogous reduction of nitrite to ammonia is a particularly difficult chemical reaction to perform synthetically in a controlled manner. Thus, her lab’s overall goal is to learn how nature evolved to do this chemistry safely and efficiently. Her work is funded by the National Science Foundation.
Support for this episode of People Behind the Science was provided by Innovative Research, Inc.
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