Bio
I was born in the small town of Sugarloaf, Pennsylvania where I lived on a small farm for my childhood with 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 tutelage of Dr. David Stiller. Each year I was there 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 skills on relating 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 due to it being a combination of engineering and biology, two subjects I was interested in and it being 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 modification of an artificial protein switch his lab developed and studying its mechanism of allostery. At this point I was hooked and found out how much I would like research to play a part in my career choice. After three years of research I was awarded the department's best undergraduate researcher and Provost's research award as well as a Master's degree. In addition to research, I spent my nights working for the intramural sports program. 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 been research a novel method of fusing proteins together after they have folded to make targeted therapeutic molecules and production of cellulases in E. coli to be used to break down grasses for biofuels. Throughout my undergraduate program, I realized how much I missed teaching and have had the opportunity to be a teaching assistant three times for an undergraduate senior laboratory and bioprocess engineering class. In the bioprocess engineering course I worked with Dr. Abe Stroock at developing the final design project as well as evaluating students on their progress throughout the class, reaffirming my desire to share knowledge with students and strengthening my own pedagogy. Outside of the laboratory and classroom I have several other hobbies including running, playing golf and tennis, and cooking CSA veggies.
Research 
The research of the DeLisa lab focuses on modifying bacteria E. coli (a non-pathogenic version of this species) to perform extraordinary tasks not normally found in these tiny cells. These projects include the production of therapeutic antibodies and creation of next generation vaccines both decorated with non-E. coli sugars (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. Our target protein to make at high titers is a cellulase enzyme. Cellulases are used in the biofuel industry as catalysts to break down the complex cell walls of plants 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 costly and difficult to culture as well as obtain large quantities of these proteins. E. coli is a often used as a protein production host due to how easy it is to grow and its ability to produce proteins at high titers; however, it does not typically make cellulases.
In our lab, using molecular cloning techniques, we are able to produce a cellulase in E. coli but since this is a non-natural enzyme it is made in low amounts. 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 incorporates changes to 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 which properties are improved rather than all-around fitness.
Random mutagenesis strategies for directed evolution often fail because these mutations are often detrimental causing the protein loosing its ability to fold and function. We use are two-tiered directed evolution strategy to solve this problem. The first step is to select for proteins that fold in E. coli since if a protein does not fold, it cannot have perform its function. We are using this selection step as a sieve to weed 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 for better-produced proteins on cellulases that fold well. However, folding does not ensure the enzyme retains its ability to break down the plant cell wall. The second step in our screen analyzes folded library members to retain cellulase activity of breaking down cellulose. Testing activity of cellulases is low throughput, 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 through the process while maintaining the activity of the enzyme (Figure 2).