Background
“One milimolar is one micromole per milliliter, which is one nmole per microliter… if you take the Km of AdoMet for LSMT and you are in a presteady state system…”When I began research in Dr. Robert Houtz’s lab in January, 2002, I heard a lot of this… very quick, concise information… but to me, mumbling that didn’t quite make sense where some words rang a bell. I felt that my year and half of college training was quite insufficient for successful discernment of Dr. Houtz’s instructions and suggestions. However, after acquiring explicit written directions of what he was trying to communicate and a little trial and error, I began to understand and flourish with scientific research.
Up to that point academically, I was one of numerous undecided college students. I had started in the Biosystems Engineering program at UK, but found this to be unaligned with my interests. Also, I knew I wasn’t “pre-med/vet/dental/ pharmacy/P.A./P.T., etc.,” which almost everyone else who studies biological sciences seems to be. However, after being fully immersed in my research and experiencing the joy of a successful, data-producing experiment, I decided that a Ph.D. followed by a teaching/research position at a large university might be the right path.
My first significant contribution to my lab’s work was in the summer of 2002. Up to that time I was learning basic skills and deciding what type of project I wanted to devote myself to. The enzyme that I work with, Rubisco Large Subunit Methyltransferase (LSMT), had been classified as containing a newly identified protein fold, the SET domain. This fold is ubiquitous to almost all organisms and is of great interest, because it is found in some proteins that influence gene silencing, chromatin formation, and certain cancers. Consequently, National Institutes of Health crystallographer, Dr. Jim Hurley, became interested in our enzyme and solved its 3-D structure. I was then able to learn first hand the difficulty and the beauty of enzyme kinetics. The lab’s efforts turned into a publication in the prestigious journal Cell, with two other crystal structures of SET domain containing proteins in the issue. A précis of the three articles clearly stated that our paper was the best (and made the cover!) due to the resolution of the structure and the extensive functional data.
There are two types of people as far as enzyme kinetics are concerned: those who understand them and those who don’t. The learning curve is steep, mainly because after fully understanding kinetic constants, which are usually denoted by k and some subscript (kcat, km, ka, kd, KD, kia, ki, etc.), you comprehend the majority of enzyme kinetics. Second, you have to learn how to interpret the complex data and be able to know when the values you obtain are reasonable or are not, a skill that develops with time. I am proud to say that I have become proficient in enzyme kinetics, which has not only trained me to be very precise, but has also helped make me become a better experimentalist.
Undergraduate research is extremely rewarding. Not only do I know a little bit about enzyme kinetics, I have been published, and have become well versed in other areas of experimental biology. I appreciate the evolution I have made as a student due to undergraduate research — now I am more analytical, critical, and capable of designing and implementing independent thought. I feel that I have gotten the most out of my education and have truly prepared myself for the next step — graduate school at the University of California at Berkeley.
Now, new students in the lab look at me in a similar, puzzled way as I did to Dr. Houtz two years ago. I take great pride in being a legitimate source of information and a person who can analyze data and teach certain skills. Furthermore, I feel lucky and humble to be on a career path that I feel confident about and drawn to; as well, I am grateful for all of the help I have received along the way.
Being awarded the Beckman scholarship has been a critical part of my growth intellectually and scientifically while an undergraduate. Receiving such a prestigious award serves as an affirmation of my abilities and a source of encouragement to achieve more, and is a great reward for all of my efforts. Furthermore, at the Beckman Symposium in the summer, 2003, I interacted with incredibly talented scientists. This provided another source of inspiration to become more proficient myself.
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