Finding My Passion For Research

My passion for research stems primarily from pure curiosity. I am constantly amazed when I think about the millions of small molecule interactions, signaling pathways, and biological phenomena that go on within us each and every day. It is these interactions that go on every second of every day behind our level of consciousness that allows us to do what we do every day. With this, I found research as a way to understand both how and why these phenomena occur.

            Though I am truly interested in many fields of science, one of my favorite subjects is molecular biology. I feel that nearly everything that happens in this world can be explained at this macromolecular level, and for this reason it was my desire to begin my research career in a laboratory that focused on molecular biology. For this reason, I felt that the lab of Dr. Islam was, and still is, the best fit for me. Every day I focus on understanding how the molecular interaction between small molecules and the class of demethylase proteins I work with allow for proper protein function. It is through studying these interactions that I have not only greatly expanded my knowledge on how to conduct research, but have more importantly grown tremendously in my passion and interest in further exploring the field of molecular biology as a way to understand how biological phenomena occur.

            If I were to give advice to a fellow student who wants to conduct research but might not know where to start, I think the best piece of advice I would give is to choose the aspect of their research interest that they are most passionate about. I believe one of the toughest aspects for me when I started research was trying pick one component of my interests and focusing solely on it. Evidently, this continues to be a problem that I deal with each and every day. For example, you can’t fully appreciate the field of neuroscience without understanding the molecular and ionic interactions that take place both within and between neurons. Similarly, you can’t fully appreciate the complexity of microbial communities without understanding the metabolic differences between different microbes and how these organisms interact spatially with each other. In short, most research is complex and necessitates an interweaving of many different disciplines. It is this reason, I believe, that most people find the field of research dauting and thus do not know where to start. Consequently, I would tell these individuals to tackle one aspect of their interests at first, and more often than not the interconnectedness with other disciplines will come naturally.

            My long-term goal is to become a physician-scientist, with my research interest focusing specifically on understanding the molecular interactions within the gut-brain axis, and clinical focus in either pathology, infectious diseases, or neurology. I believe that one of the biggest challenges in becoming a physician-scientist centers around balancing both the clinical and bench side aspects of work. It is thus critical to foster relationships and connections in both realms that allows me to more easily balance both these aspects of my career. In the lab, I would obviously need to build a lab group (or just work in someone else’s lab) that has individuals that can assist me in my work if I am occupied in the clinic and may not be able to focus as much time in a given work on my research project. On the other side, I believe that becoming nearly any physician, not just a physician-scientist, necessitates a whole cohort of individuals to effectively schedule appointments, offer differing diagnosis on patients, and much more. As a result, I fully expect the need to build these communities with coworkers in order to become an effective physician-scientist.

Shown in the figure above is a simple schematic illustrating part of my research project. Show in panel (A) is the chemical structure of the FTO inhibitor, NOG. This is a structural analogue of the FTO activator 2-KG, which is shown in (C). Shown in (B) is a structural representation of NOG-bound FTO, depicting some of the amino acids that interact with NOG (and subsequently 2-KG as well, as they both compete for the same active site). Finally, in panel (C) and (D), a schematic representation of the bump-hole assay is shown. The hole modified FTO harboring a silent mutation can bind native 2-KG and perform its WT demethylation ability (as shown in (C)), but it is no longer inhibited by native NOG (not depicted). However, by chemically adding small ‘bumps’, or chemical side chains, to NOG that can bind to and fill the ‘hole’ of the FTO mutant, inhibition of the FTO is restored (as depicted in (D)).

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