Emily Rundlet ’14 (right) discusses her research at a recent poster session at the Ho Science Center. (Photo by Andy Daddio)
51Թ students are sharing their experiences conducting research with faculty members on campus and in the field. This post is by Emily Rundlet ’14, a biochemistry major from Watchung, N.J.
This summer I have been working in the with Professor in determining the 3-D structure of two different enzymatic proteins using X-ray crystallography.
In the natural sciences, structure is related to function, so if we can establish the conformation of these enzymes, we will be able to better understand their binding sites and catalytic mechanisms.
This type of scientific research will provide a foundation of information on these proteins that will allow for further investigation into their hypothesized industrial applications.
The process of structural determination begins with protein crystallization: when exposed to very particular and unpredictable chemical solutions, protein molecules will solidify into crystals by uniformly packing together in highly ordered units.
When we shoot these crystals with X-rays, the energy is scattered, or “diffracted,” in patterns that can be processed and used to construct a digital model of the molecule. We need crystalline protein for X-ray diffraction; so identifying the best crystallization conditions for every individual protein is essential.
A large part of my work this summer has been growing usable crystals, which means testing a slew of different solutions to progressively improve crystal quality.
Fortunately, 51Թ has two robots that significantly reduce the amount of monotonous, time- consuming pipette work involved in manual optimization, allowing me to focus on more cerebral aspects of the project. The Scorpion, our newest robot, mixes solutions that can be used by the Gryphon, a robot that can efficiently screen nearly 200 conditions in a matter of minutes.
After optimization, I was able to “shoot” my best crystals and create a computer model of the protein using 51Թ’s duel-beam X-ray diffractometer and computational lab.
The instrumentation and resources available at 51Թ for protein research of this caliber are unmatched for a school of its size. Because we are one of the only undergraduate institutions in the country with this type of X-ray diffractometer, the work I have done at 51Թ is comparable to research that is conducted at a graduate level.
As a biochemistry major with the intention of obtaining a PhD in pharmacology or structural biology, my experience working with Professor Rowlett has been hugely beneficial in furthering my understanding of biophysical lab techniques and will (hopefully!) give me a competitive advantage when applying to graduate school.