After three hours in airports, thirteen hours in the air, two busses, one train and five flights of stairs carrying 100 lbs of suitcase, I had finally arrived. My summer abroad in Copenhagen, Denmark was to be quite an adventure and an experience that would stretch me both as a scientist and as a person.

Having never traveled overseas before, the first couple days were quite an adjustment. Everything around me was unfamiliar and I often felt like I was wearing a sign that stated in bright, bold letters: "yes I know, I'm foreign." Cycling is an integral part of life in Copenhagen. So, I acquired a rusted, old bike and took to the bike lanes. I must say that biking in the city is no easy task. It is fast paced, and one must be ready at all times to avoid the biker who stops suddenly in your path, quickly veer onto the sidewalk when the bike lane is under construction, and avoid the multitudes of people who walk directly in front of you without looking. I had a few near death experiences, but managed to escape the summer with only a bruise or two. The flat I rented was located about four miles from the lab. My route to work took me down one of the busiest streets in the city, so needless to say I was very awake by the time I arrived at the lab!

I worked in the Laboratory for Molecular Pharmacology at the University of Copenhagen under the supervision of Dr. Thue Schwartz. Surprisingly, I was one of only four foreigners in a lab numbering approximately 20 people. Everyone that I worked with spoke English fluently (I would often joke that their English was better than my own!); yet in spite of this I found the language barrier to be quite an obstacle. Danish was the primary language spoken in the lab, and very understandably others would not switch from their native language to English merely because I joined them. In the beginning of my summer I often felt like I was present physically, but not connecting with people emotionally. This just meant I needed to be creative. I soon realized that food was a very social thing in Denmark; so to remedy this disconnect, I would bring in fresh baked bread in the mornings. People would stop their work and flock to the table, where we would all sit around and talk. The lab also shared breakfast together on Monday mornings, and this was a great way to foster community among the lab members.

As time went on I felt much more welcomed and accepted by my coworkers. For the 4th of July I planned a Summer S'mores Party, as we called it, to introduce the lab to the art of making a proper s'more. The party became a funny topic of conversation throughout the month of June. Everyone joined in; a few technicians even brought in a variety of sample chocolate so that we could decide which would be the best s'more material. The party went very well! It was fun to be able to share a bit of American culture with them, and so nice to feel more connected to people in the lab. I would say that was a turning point for the summer in terms of relating to my colleagues.

The Schwartz lab is primarily focused on characterizing seven transmembrane G protein coupled receptors (7TM GPCRs). They seek to gain a better understanding of how the ligands for these receptors bind and activate 7TM receptors, and how this leads to signal transduction. My work in the lab was two-fold. I worked with two 7TM receptors that both belong to the ghrelin subfamily. Ghrelin is a hormone that serves as a hunger signal from the upper GI track to the central nervous system. The ghrelin receptor is expressed in the hypothalamus and is involved in regulating feeding behavior and energy homeostasis. While mutational analysis has revealed which amino acid residues on the ghrelin receptor are important for receptor activity, it is not yet possible to determine the orientation of the ligand in the binding pocket. Using methane thiosulfonate (MTS) derivatives, we attempted to map which residues in the binding pocket were on the water accessible surface of the protein. We made a series of ghrelin mutants in which residues were mutated to cysteines. We then treated the receptor with the MTS derivative and afterward carried out competitive binding experiments with radiolabled and unlabled ghrelin. The MTS compound would only be able to react with the mutated Cys residue if the residue was accessible in binding pocket. Second, we hoped to determine the orientation of the ligand in the binding pocket by covalently attaching an activated thiol group to one end of the ligand. The intention was that the reactivity of this ligand would be guided by its natural affinity for the receptor. Once bound in the binding pocket of the receptor the reactive thiol group would form a disulfide bridge with the mutated Cys residue. Unfortunately, we were not able to elucidate any information about the orientation of the ligand because the thiol chemistry was too strong and reacted with each of the mutated Cys residues in every area of the pocket.

My second project involved the orphan 7TM receptor GPR39. It was proposed that GPR39 serves to protect the cells against reactive oxygen species. I first learned the molecular biology necessary to make a stable clone of GPR39 and a GPR39 mutant in an inducible FLP-In T-REx cell line. Once the cells line was functional, I carried out a series of viability assays to test this hypothesis.

As a whole, I really enjoyed my experience in the lab. Though it took some time to build relationships with people, by the end, it felt like we were a small family. I would like to give a special thanks to Dr. Thue Schwartz and all those in the laboratory who made my experience very memorable. I would also like to thank Carol Bender and the BRAVO! program for making this opportunity possible.

Erin Palmer, UBRPer in Dr. Victor Hruby's laboratory, Chemistry

NOTE: Watch for Erin's datablitz as well as others given by the Summer 2007 BRAVO! Participants