ALUMNI/AE SPOTLIGHT - Annie Schafer ’18

nnie Schafer ’18 is a recent Clark University graduate, earning a master of science in Biochemistry and Molecular Biology. She traces her love for science back to her days at Eagle Hill School. “It wasn’t until I started working in the biology lab at Eagle Hill, where I discovered my passion for science, that I truly felt like I belonged somewhere,” stated Annie.

Like most students when they first visited the campus of Eagle Hill School, Annie Schafer had no idea what her future would hold. However, shortly after arriving, Annie discovered that she thrived in the science department, especially in the biology lab, under the supervision of Mr. Ward (biology teacher). As a master’s graduate, Annie was ready to reflect on some of her early struggles with her diverse learning profile. She hopes that sharing her story will inspire other Eagle Hill students to persevere through their challenges.

Annie especially struggled with test taking while an Eagle Hill School student. “I took the ACT three times while attending Eagle Hill. I got the same score twice, and then on the third time, I dropped two points. It wasn’t as if I did horrible, but I didn’t do great either.

“It was consistent with what I had been trying to overcompensate for my whole academic career leading up to that point. I knew that the knowledge I accumulated over the past four years didn’t reflect the humanization of knowledge I gained while attending Eagle Hill School. I was worried that I would not be able to attend a prestigious college like some of my peers. Fortunately, while going through the college advising process and with the help of EHS’s college counseling department, I was accepted into Clark University, where I graduated with my master’s degree just this past May,” stated Annie.

Before graduating from Eagle Hill School, Annie learned to embrace her diverse learning profile and was shown how to use her unique learning style to her benefit. These gifts became her most significant strengths, and while attending Clark University, she fully leaned into them.

“You know, science is very strict, but you also have that creative freedom to try and solve a problem differently. I compare it to learning differently.

“For example, there are multiple ways to make a peanut butter and jelly sandwich. One person might make it with two slices of bread, and one person might make it while using one slice of bread, but in the end, you both end up with a sandwich. I think my best piece of advice is to follow your individuality. It’s very important as a person in science that you can work well with your classmates or colleagues to collaborate on the same project. At the same time, I think knowing when to separate yourself on your own terms is equally important.

“When I was learning all the different scientific techniques in the Spratt Lab at Clark University, it took me more time to learn, understand, and grasp all these different concepts we were being taught. People at times may get annoyed with you; they may wish that you could pick up the material faster; however, in the end, take your time, own your learning differences, and always stand up in the face of adversity.

“Another piece of advice I would give EHS students coming into the STEM field is not to be afraid of being wrong. I think we all strive hard to be perfect, but in this field, you have to be wrong to learn and grow as a scientist. If you happen to get it right on the first try, that’s great, but more often, when you get things wrong and learn how to do it right, you tend never to forget how you came to that final solution,” concluded Annie.

Before Annie graduated from Clark University in May, she invited Mr. Ward’s IB Biology class to the Spratt Lab. The

Research In The Spratt Lab

The regulation of enzyme catalysis and protein function resulting from the specific interactions between two or more proteins plays an integral role in cell division and homeostasis. The development of various human diseases can occur when these proteinprotein interactions are disrupted or modified. Understanding how these protein-protein interactions affect an enzyme’s ability to make or break bonds and its underlying mechanism is an important step in drug design/development.

Ubiquitylation involves the transfer of the small 76-residue protein ubiquitin between a series of enzymes (E1, E2, E3) until it labels the ε-amino group of a lysine residue on a substrate protein. This pathway is involved in many different intracellular processes including protein turnover, cell cycle progression, signal transduction, DNA repair and transcriptional regulation.

The research program focuses on deciphering the unique mechanisms employed by members of the HECT (Homologous to E6AP Carboxyl Terminus) E3 ubiquitin ligase students had the opportunity to isolate fluorescent proteins with the assistance of Annie’s professor Dr. Spratt. After the experiment, the students also participated in an interactive discussion about career paths in STEM and got a private tour of the facilities from Annie herself. family. Working at the interface of physical biochemistry and chemical biology, the research team uses biochemical and biophysical techniques including NMR spectroscopy to understand how HECT E3 ubiquitin ligases attach ubiquitin or ubiquitin-like proteins to a substrate protein. Specifically, the group is focused on the following themes:

Now that Annie has earned her master’s degree, she has signed a two-year contract with the National Institute of Health, working at the National Cancer Institute out of Bethesda, MD. Her work will focus predominantly on blood cancers and the specific protein’s overall structure to determine their function, discrepancies, and disparities.

As Annie starts her career in STEM, we thank her for being an excellent example of what it means to be a Pioneer.

• Molecular basis for specificity in ubiquitin chain linkage by the HECT E3 ligases

• Mechanism and ubiquitin handling by the HECT E3 ligases

• Substrate recognition by the HECT E3 ligases

These studies will help to clarify how HECT E3 ligases form multi-protein complexes to build ubiquitin chains and how the malfunction of these complexes cause various human diseases.

Reference: Clark University, The Spratt Lab. “Research”, 2019, https://wordpress.clarku.edu/ dspratt/research/

1970

John Barry

John Barry, 1970, stopped by campus with his wife and good friend. They enjoyed a tour given by the director of admission, Dana Harbert. John could see firsthand all the incredible progress made to the school since he graduated from Eagle Hill School.

1977

Drew Fernandez

Drew Fernandez, 1977, stopped by campus with his son while driving back to their home in Newport, RI. Director of Admission

Dana Harbert and Associate Director of Development Brooke Epstein walked them around campus for a grand tour of all the new buildings. Drew and his son were amazed at the progress made since he graduated from Eagle Hill School.