Graduate Student Highlight: Ian Sitarik
Each week, the Department of Chemistry highlights a graduate student who is doing interesting and exciting work within the department. In this installment of our highlight series, we are featuring Ian Sitarik, who is a fourth-year student in the O’Brien lab.
Ian uses a combination of computational protein models and experiments to understand the fundamental principles driving protein folding and function within the cell. This combination allows him to make educated predictions about what genetic modifications may increase or decrease the structural integrity and functional capacity of various proteins and then test those predictions in the real world using the full force of Penn State’s core facilities.
Outside of the lab, Ian is part of an unofficial hiking club that has members from various departments around the University. The club goes hiking weekly in the beautiful state parks surrounding State College.
This week, we met virtually with Ian to discuss his life in and outside of the lab! Please enjoy our interview with Ian Sitarik.
Question: How did you get interested in chemistry?
Answer: I got interested in chemistry for two reasons: One, it makes me feel more at ease when I understand what matter is doing around me. I mean, come on, it’s everywhere, and most people know nothing about it. That should terrify them as it did me when I was a kid! Two, it is one of the most versatile degrees you can get, allowing for entry into multiple job markets.
Q: What inspires you as a scientist?
A: To be honest, it’s the uncertainty. Once I found out that nothing in science was absolute (we can debate about scientific laws), I became obsessed with trying to understand how we can quantify nature with a precision and accuracy that is acceptable enough to have some level of certainty.
Q: What accomplishment are you most proud of? (Either as a scientist, or otherwise)
A: Surviving a midwest military boarding school for six years and then making it through to being a PhD candidate at one of the top twenty universities in the country! It's been a long road.
Q: Why did you decide to come to Penn State?
A: I came to Penn State because it’s one of the top twenty universities with a biophysical-oriented chemistry department, and it’s the only one located between two state parks with tons of hiking and outdoor activities.
Q: Where did you grow up? (Tell us a fun fact about your hometown if you want)
A: I grew up in a medium-sized city one hour north of Denver, Colorado called Fort Collins. It's right along the front range of the Rocky Mountains, so I would be lying if I said I didn’t miss seeing those massive, snow-covered peaks every day. Downtown Fort Collins was actually the inspiration for Disneyland's Main Street USA. Many of the same buildings that were used as models by the Disney imaginers still stand.
Q: Do you have any hobbies?
A: I have many, but not enough time to devote to them because of graduate school. I draw and write fiction and am part of avid artist communities online. I hike a lot, at least once a week. Games are a given, but only for one hour a week on the weekends sadly.
Q: Do you have any pets?
A: I have one stray cat that I adopted exactly one year ago named Mue. He is a bundle of love with claws.
Q: What’s your favorite way to spend a day off?
A: Hiking with friends followed by games and drawing.
Q: What’s your dream vacation?
A: Kayaking in Alaska followed by a trip around the Pacific Rim.
Q: What’s your favorite book or movie?
A: Ten years later The Divine Comedy still gives me a fresh perspective every time I read it.
Q: If you could have dinner with anybody (living or dead), who would it be and why? (And what would you eat?)
A: To be honest Jesus. For many reasons, but if one person's name echoes so far and loud through history, they must be interesting to talk to. We would eat sushi followed by vintage wine and dark chocolate.
Bonus Question: Do you have any fun science trivia to share?
A: Q- Can proteins have multiple unique structures for the same amino acid sequence?
A- Yes, they are called folding switching proteins that can modulate between two (or more) different unique tertiary structures given different chemical conditions.
Thanks to Ian for these interesting and thoughtful answers! We hope you enjoyed this interview. Stay tuned for more graduate student highlights in the weeks to come!