By Sarah Fine (’16)

Sarah Fine

We are each here – alive and awake – because our bodies are maintaining a favorable environment for appropriate enzymatic activity. Enzymes are proteins that speed up reactions to rates that are fast enough to sustain life; essentially, enzymes make it possible for our bodies to transform what we have into what we need.

Much like the human body, Wake Forest is a vessel of transformation. Every year, hundreds of new substrates enroll, while hundreds of new products graduate. Along the way, we develop into new, better, versions of ourselves. So, what really changes us? How is Wake Forest able to radically enhance our approaches, our world views, our passions in such a short period of time?

I hypothesize that these changes are due to the enzymatic activity at play on this campus. Perhaps it was the RA who kept you company during a difficult time who inspired you to become an RA yourself. Perhaps it was the student organization that introduced to your passion that encouraged you to serve in a leadership role. Perhaps it was the professor who challenged you to think beyond the text who moved you to declare a certain major. Perhaps it was the Wake Forest tradition that made you smile or laugh or cry that motivated you to create a new Wake Forest tradition. Perhaps it was the friend who accompanied you on that midnight run to Cookout who influenced you not to transfer. Perhaps it was the study abroad program that immersed you in a culture different from your own that stirred you to think more globally. Perhaps it was the university office that felt like home that empowered you to be true to yourself. Perhaps it was the assigned reading that contradicted your strongest beliefs that energized you to consider an alternative perspective. Or, perhaps it was the Biochemistry class that provoked you to think critically about enzymatic activity that prompted you to write a senior oration about enzymes. In any case, something or someone made it possible for you to convert what you brought to this campus into what you are taking away.

But how exactly does this happen? Two models have been proposed to help explain the mechanism by which enzymes catalyze change. The Lock and Key Model proposes that a substrate acts like a key, physically and chemically complementing an enzyme’s lock. However, this model is widely rejected: if a key fits into a lock perfectly, why would the lock work to change the key at all? The more accepted Induced Fit Model postulates that an enzyme binds to a substrate that is only semi-complementary. In this model, the enzyme strains the substrate, and the substrate strains the enzyme. In essence, they make each other uncomfortable and induce physical and chemical changes until they fit each other a little better. Finally, the product is formed, and the enzyme releases the product. The enzyme is finally available for another reaction. In many ways this mirrors our relationship with Wake Forest.

For many of us, our first days as Demon Deacons were challenging. We were well beyond our comfort zones, and we strained to find our place. Suddenly, we were not the only valedictorians or class presidents or star performers. We realized Wake Forest was not our perfect compliment. Over the past four years this campus has challenged us and we have challenged this campus. We have both been transformed. Finally, it is time for us to be released, and for our enzymes to be regenerated. As we graduate, we leave behind these halls, these classrooms, these professors for the next group of substrates to begin their journey. Herein lies a deviation from this analogy: our enzymes are not restored perfectly back to their original states. Each one of us has left a permanent impact on this campus, on our enzymes – an impact that hopefully strengthens their drive to help the next round of students.

It is important to note that enzymes function with great levels of specificity. They do not follow a one-size-fits all standard. Each enzyme catalyzes a unique reaction, and binds only to a specific substrate. As such, each of our Wake Forest experiences is incredibly unique. Each of us was a unique substrate that required a unique set of enzymes to perform a unique set of reactions. It is the collaboration of the products we have become that allows the world to flourish.

There are approximately 75,000 different enzymes in the human body. Exclusion of even a single enzyme could result in severe illness. The buildup of a particular substrate and lack of a particular product could manifest in a life-threatening disease. Similarly, our world will only prosper if all substrates, all people, are given the opportunities and support that they need to succeed. That said, we cannot expect new varieties of substrates to fit into the preexisting enzymes on this campus. While it is important that we welcome a greater diversity of students, it is equally crucial that we provide each of them with appropriate resources.

However, we cannot merely implant new enzymes, and expect them to thrive. All enzymes require distinct environmental conditions. Digestive enzymes of the stomach, for example, require a low pH to function properly. If one were transplanted to the blood, it would likely stop working and be destroyed because of the much higher pH found in the blood stream.

Likewise, simply introducing new resources is not enough. We need to change our environment so that these resource feel both safe and welcomed. We change our environment by choosing inclusive language, by hosting accessible events, by encouraging productive decisions, by celebrating difference. We change our environment by recognizing that the fish’s ability to swim is just as incredible as the cheetah’s ability to climb a tree. We change our environment by being deliberate in the conversations we have, by listening, by sharing, by nurturing.

We are not finished transforming, nor should we ever be. Like molecules in the body, we will constantly change from what we have into what we need, and along the process, we can create a more conducive atmosphere for a wider range of humanitate.