Bio
I was born in the small town of Sugarloaf, Pennsylvania where I lived on a farm for my childhood with my parents and younger sister. I attended MMI Preparatory School for middle and high school. It was there that I gained my passion for research and teaching under the supervision of Dr. David Stiller. Each year, I presented research at the Pennsylvania Junior Academy of Science (PJAS) on topics ranging from determining friction coefficients for tires, to killing termites with antibiotics. I found the scientific process extremely exciting and learned how to present my research to peers. In addition to PJAS, I actively tutored my fellow students in high school. I gained the skill to relate subjects to my friends and found out how rewarding it was to master a subject. It was then that I decided I would like to attend graduate school. In addition to those activities, I was also a member of Boy Scout Troop 207 where I earned the rank of Eagle Scout with the help of my scoutmaster, C. Wayne Oberst. I played varsity tennis all four years of high school and was the valedictorian of my class.
My desire to do research led me to attend the Johns Hopkins University for my undergraduate studies. I decided to study Biomolecular Engineering at Hopkins as it combined engineering and biology, two subjects that interested me, and it was a unique way to study both. I started working with Dr. Marc Ostermeier in my sophomore year in his protein engineering lab. My research there focused on modifying an artificial protein switch his lab had developed and studying its mechanism of allostery, the regulation of protein activity through interactions away from its active site. At this point, I was hooked and certain that I would like research to play a prominent role in my career beyond simply attending graduate school. After three years of research, I was given the department’s best undergraduate researcher and Provost’s research award, as well as earned my Master’s degree. In addition to research, I spent my nights working for the intramural athletics program officiating and managing various sports such as basketball and volleyball.
I decided to attend Cornell University after graduating from Hopkins to continue working on Biomolecular Engineering problems under the tutelage of Dr. Matt DeLisa. Over the past five years, I have worked on two projects, one being a novel method of fusing proteins together after they have folded to make targeted therapeutic molecules, and the second producing cellulases in E. coli to break down grasses for biofuels. Throughout my undergraduate program, I realized how much I missed teaching, so I welcomed the opportunity to be a teaching assistant three times for an undergraduate senior laboratory and bioprocess engineering class. In a bioprocess engineering course, I worked with Dr. Abe Stroock to develop the final design project as well as evaluating students on their progress throughout the class. This reaffirmed my desire to share knowledge with students and strengthened my own pedagogy. Outside of the laboratory and classroom I have several other hobbies including running, hanging out with friends, playing golf and tennis, and cooking CSA veggies.
Research 
Cellulose, or the material that structures plant cell walls, is the world’s most abundant form of biomass. As such, it is a popular target for researchers trying to break down this compound to serve as a precursor to renewable biofuels. Cellulases are used as catalysts to break down the recalcitrant cellulose into simple sugars. These sugars are fed to other organisms (e.g., yeast) to create ethanol-based biofuels. Cellulase enzymes are commonly produced from fungal extracts that are challenging to culture in large amounts and costly to grow. The bacterium E. coli (a non-pathogenic version of this species) is often used as a protein production host because it is easy to grow and for its ability to produce proteins at high titers. However, it does not typically make cellulases. The research of the DeLisa lab focuses on modifying E. coli to perform extraordinary tasks not normally found in these tiny cells; see http://www.cbe.cornell.edu/~md255/DLRG/Research.html. The goal of my project is to utilize the natural pathways found in E. coli to expand the engineering potential of this organism for greater production of industrially relevant products, such as cellulases.
In our lab, using molecular cloning techniques, we are able to produce a cellulase in E. coli, but only in small amounts, given that it is not a natural enzyme. To solve this problem, we created a two-tiered directed evolution strategy (Figure 1) utilizing some of the natural abilities of E. coli. Directed evolution is a common technique to find protein variants, from a random mutagenesis library, with desired properties such as increased production. Random mutagenesis changes the primary amino acid sequence of the parent cellulase protein. This method of random mutagenesis followed by selection for desired properties is akin to natural evolution processes to find the fittest members of a population. However, by controlling the selection step in the laboratory, we can focus on which properties are improved, rather than all-around fitness.
Random mutagenesis strategies for directed evolution often fail because these mutations cause the protein to lose its ability to fold and function. We use a two-tiered directed evolution strategy to solve this problem. The first step is to select proteins that fold in E. coli, since if a protein does not fold it cannot perform its function. We are using this selection step as a sieve to filter out all the non-folded members from a random mutagenesis library of cellulase enzymes. To accomplish this, we take advantage of a pathway found in E. coli that discriminates between folded and non-folded protein. Using this natural quality control mechanism, we can focus our search on better-produced proteins on cellulases that fold well. However, folding does not ensure that the enzyme retains its ability to break down the plant cell wall. The second step in our screen analyzes folded library members that retain the cellulase activity of breaking down cellulose. Testing the activity of cellulases is a low throughput process, but our pre-selection for folded members focuses this step on only enzymes that have a high likelihood of retaining enzymatic activity. Using this strategy, we have increased the production of our cellulase in E. coli by 10-fold in just two iterations while maintaining enzyme activity (Figure 2). In the future, we hope to improve the production of other cellulases with our two-tiered strategy, and determine how the quality control mechanism selects for well-folded proteins to allow this method to be broadly applied to other proteins.