Lexie Kuzmishin Nagy photo

Lexie Kuzmishin Nagy, Ph.D.

Assistant professor of biochemistry

Email:[email protected]

Location: Stanley Hall 237
801 National Road W
Richmond, IN 47374

About me

I am a biochemist interested in how bacteria maintain and edit their proteins during stress using aminoacyl-tRNAs. I contribute to courses in the Department of Biology, Department of Chemistry, and Biochemistry major. When I’m not teaching or researching, I like hiking or generally spending time outside, usually with my husband. When not outside, you can find me playing video games or board games, or reading in the company of my two cats, Ruckus and Ruffle.

I teach at Earlham College because it is a wonderful place with a rich history in advancing justice, diversity, equity, and inclusion initiatives and a community who values that history and embodies its core principles. My colleagues challenge me to think creatively about both my teaching and research, and support my endeavors to try new techniques and explore new ideas. Although I have not been here long, it’s clear to me that Earlham is a community of learners that support and encourage each other to grow and be intentional about our actions and presence in the world.


  • NIH IRACDA Postdoctoral Fellow, Emory University
  • Ph.D., Biochemistry, The Ohio State University
  • B.A., Biochemistry & Molecular Biology, The College of Wooster

Professional memberships

Research projects

Amino acids are the building blocks of proteins; multiple amino acids bond together to form a complete protein. The chemical properties of each amino acid impact the overall shape and, therefore, activity of a protein. Aminoacyl-tRNAs deliver amino acids to the growing protein chain, and play an important role in ensuring the correct amino acid is delivered at the correct time. However, environmental and cellular stresses can cause aminoacyl-tRNAs to deliver the wrong amino or can damage amino acids in a way that alter their chemical properties. How do bacteria detect these changes to amino acids or mistakes in amino acid delivery? How do bacteria fix them? These are questions my research seeks to answer using techniques from biochemistry, molecular biology, and microbiology.

Specifically, L-amino acids have a particular geometric arrangement that allows them to be used in proteins, whereas the opposite configuration of D-amino acids prevents their use in proteins. Aminoacyl-tRNAs carrying D-amino acids are toxic to bacteria, likely because they prevent proteins from forming correctly. My current research uses several bacterial models, including E. coli and R. palustris, to investigate how bacteria use enzymes, called trans-editing proteins, to find and fix aminoacyl-tRNAs carrying D-amino acids.

Interested? Consider joining me in a collaborative research experience!

Scholarly interest

I am interested in how bacteria act upon aminoacyl-tRNAs to respond to different stresses, and the effects on bacterial protein structure and activity. As a biochemist, I ask questions about the relationship between the structure and function of molecules, which allows me to apply both chemical and biological concepts and skills in my research. Therefore, my interests are quite broad: I am interested in questions about how proteins fold, how proteins engage their targets in the cell, and how the sequence and organization of a gene (DNA) impacts the production of the RNA required for subsequent protein synthesis (“gene expression”).

I am also interested in how the life sciences (chemistry, biology, biochemistry, and the associated sub-fields) intersect with society. The advent of public-facing genome sequencing services, such as Ancestry.com, is one example. How does the availability of genetic information affect healthcare; crime solving; our understanding of family history? Science doesn’t exist in a vacuum; understanding how our discoveries and technologies impact societies is just as important as the science itself.

Published works

A full list of publications can be found on my Google Scholar profile.

We continue to monitor the effects of an industrial fire 1.1 miles from campus.
We continue to monitor the effects of an industrial fire 1.1 miles from campus.