Wednesday, June 30, 2010

Greetings fellow scientists, science-enthusiasts, and LabSpaces paparazzi! For those who don’t know me from my *ehem* Twitter omnipresence, I thought I’d share a little about myself and how I ended up in a career commonly—and often appropriately—preceded by the word “mad.” If you do know me, don’t zone out just yet. You may discover something new, and this material might be on tomorrow’s pop quiz...

My infatuation with science began when I was young and fancied myself as something of an athlete. During high school, I played three sports, in addition to participating in a bevy of other extracurricular activities. Keeping up with athletic practice, homework, and a smattering of social events took an incredible amount of energy. I became interested in nutrition, which I saw at the time as a way to optimize the ratio of energy generated vs time spent eating. (Note that there were many flaws in the design of this study. The most important flaw was that, like most teenagers, I neglected to include the variable now known to me as “sleep” in the equation. Though the wisdom of age has made me aware of its importance, I continue to convince myself at times that its correlation coefficient is 0.)

As I studied nutrition and learned about the role of proteins, carbohydrates, and fats in the body’s catabolic and anabolic processes, I continually felt like I was being shammed. I felt there had to more to this hodgepodge of long chemical names and how they were turned into muscle and fat cells than I was being told. I wanted to know more. I wanted details.

Enter: college biochemistry. I was hooked after only a couple weeks of learning about the synthesis of amino acids from various precursors and how these amino acids were combined to produce, among other things, enzymes. For your enjoyment, I’ve included a picture of my favorite enzyme from college biochemistry, Triose Phosphate Isomerase (TIM). I adore TIM because it is an example of what I attempted—and failed—to achieve with my teenage nutrition experiment: catalytic perfection. In enzymology, this term means that TIM’s productivity is limited only by “external” factors, such as the binding of substrate, rather than its own ability to catalyze the reaction.

Fast forward to today. I’ve expanded my list of cool biomacromolecules to include those composed of nucleic acids, but I’m still big on the details. My research focuses heavily on a technique, Nuclear Magnetic Resonance (NMR), that provides atomic resolution information about the system of interest. Specifically, I use NMR to understand the way in which biomacromolecules, including enzymes, move. This movement is critical to a variety of processes, including catalysis of reactions, the binding of drugs, and the communication of signals from external stimuli inside a cell. You know, pretty much everything that makes life possible.

Related Links:
1. RCSB Protein Data Bank entry for the crystal structure of Triose Phosphate Isomerase.
2. Journal article reporting the structure of Triose Phsphate Isomerase: Kinoshita, T., Maruki, R., Warizaya, M., Nakajima, H., & Nishimura, S., 2005, Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 61(Pt 4), pp. 346-9.