Franklin & Marshall College Franklin & Marshall College

Scott Brewer

Undergraduate Research with Dr. Brewer by Emily Smith '11 

I began my research experience with Dr. Scott Brewer working as a Hackman Scholar on a project the summer following my sophomore year. I was a newly declared Chemistry major and having just completed my two semesters of Organic Chemistry, I was eager to try my hand at some out-of-the-classroom laboratory work.  I began synthesizing unnatural amino acids, specifically para-ethynylphenylalanine.  Theoretically, it was a small, smooth step from Organic Chemistry 2 to a ten-step synthesis project, but I recall feeling overwhelmed and even a bit lost.  Forty hours a week of lab time in comparison with four hours is quite a leap, and the challenge and responsibility of working on publishable material is initially a little terrifying.  However, my memories from that first summer are nothing less than positive and I owe much of them to the superior support from Dr. Brewer and my senior lab members. It is both unbelievable and invaluable the extent to which my lab technique improved over the course of merely one summer.

I spent my junior spring semester working on a one-semester continuation of the research I began the previous summer, which rolled into another summer spent in the lab and effortlessly into my yearlong independent study with Dr. Brewer to round out my senior year.  Today, I have a comfort in the laboratory that goes beyond which one can gain from a class. 

One of the aspects of my independent research I appreciate the most is the wide range of chemistry I have the opportunity to practice.  It began with organic synthesis of isotopically labeled unnatural amino acids—a great place to start when I had not yet completed any advanced Chemistry courses.  I then incorporated these unnatural amino acids site-specifically in protein systems, primarily superfolder green fluorescent protein (sfGFP), and developed new sites in sfGFP for mutagenesis via overlap polymerase chain reaction.  The free amino acids as well as the mutant protein constructs were analyzed using NMR and IR spectroscopy.  Therefore, over the course of the work I have done and continue to do with Dr. Brewer, I have had the opportunity to conduct research in Organic, Physical, and Biochemistry.

In addition to the development of new and old laboratory techniques, I have gained a level of confidence and academic understanding that I will surely take with me to future endeavors.  Recently a paper from my lab group, of which I am first author, “Probing Local Environments with the Infrared Probe: L-4-Nitrophenylalanine,” has been accepted to be published early this spring in The Journal of Physical Chemistry B.  In addition, I am presenting a poster on the findings of this paper and current works at the Biophysical Society Annual Meeting in Baltimore, MD and the American Chemical Society National Meeting in Anaheim, CA.  With these new developments underway, I continue to investigate the use of other isotopically labeled unnatural amino acids as spectroscopic probes of local protein structure and environment, such as C13O18-para-iodophenylalanine and deuterium-labeled para-ethynylphenyl-alanine.

I found research to be a fantastic way to integrate all of my experiences in the Chemistry Department.  The guidance I have received from Dr. Brewer over the course of my research has made me not only a better scientist and enriched my understanding of Chemistry, but a more confident and stronger student.

    • Emily Smith and Dr. Brewer