Undergraduate Research
Science Journal, Fall 1997 -- Vol 15, No. 1
Snap. Crackle. Pop. The noises come not from a cereal bowl, but from a 10-by-10 inch Plexiglas cube, the cramped abode of a thousand fruit flies. One side is covered with a large piece of mesh that, if you lean your ear close enough, transmits the clamorous hum of two thousand wings beating. The scientific name for these fruit flies is Drosophila melanogaster, and they are in the box because flies are good models for understanding how organisms develop. Mike Goller '97 B.S. MCB, an intense, dark-haired twenty-year-old from Long Island, sets the flies aside and tells a molecular mystery story with the competent assuredness of a post-doctoral research scientist.
But Goller has yet to earn a Bachelor's degree. He is one of many Penn State Eberly College of Science undergraduates who is committed to learning science by doing science. "Penn State undergrads are really very good in the laboratory," says Professor of Biochemistry Gregory Farber, "As good as graduate students in many cases." Talk with some of these students and you'll find an enthusiastic commitment to undergraduate research.
Goller has discovered a lot about science during his six semesters working with Assistant Professor of Biochemistry and Molecular Biology Esther Siegfried. He's especially learned that he wants a life in research, despite the difficulties of obtaining research funding. "There are a lot of things to push you away from research now," says Goller, "But I think if you really believe in science and if you have an honest interest in answering difficult questions, then doing science is just very compelling and you kind of lose sight of the drawbacks." The difficult question that occupies him is this: how does a single cell, so tiny you need a microscope to see it, turn into a whole organism? Goller is working to build a bridge, plank by plank, over the developmental gap between the microscopic cell and the menacing fly invading your bananas.
A cluster of cells can't form wings or ten distinct fingers without good communication. Couriers are needed to deliver messages from outside the cell to molecules inside, a process called signal transduction. Goller focuses on understanding one of these middlemen named zeste white 3 (zw3). Like Paul Revere spreading the news he received from the light house, zw3 first receives a sign, then dispatches that signal to other molecules that ultimately turn genes on or off. The challenge is to find that initial signaler and to track zw3 to its targets. Goller looks for these molecules in yeast cells using protein interaction screens. Even if he doesn't find any significant members of the zw3 signaling pathway, Goller, a recipient of the prestigious Goldwater Scholarship, won't consider his time wasted, "I learned so much along the way," he says.
Another undergraduate researcher, John Strothers '96 B.S. PM, B.A. Hist, shares this sentiment. Strothers, a tall, blond, baritone-horn player in Penn State's Blue Band, has spent five semesters working with Professor of Dairy and Animal Science Daniel Deaver. "I am really glad I did research for kind of a funny reason," Strothers confides. "Despite the fact that I really enjoy working here in the lab, I've discovered that I want to go into medicine and work with patients." He explains that if he hadn't done research, he would've been unable to make an educated decision about a career path. Strothers also partially attributes several achievements to his research experience, including admission to Hershey Medical Center and an Air Force Health Professions Scholarship. Participation in Penn State's Undergraduate Research Fair and the annual National Conference on Undergraduate Research has allowed Strothers to present his project to his peers.
Strothers works on bovine growth hormone (GH), a pituitary-gland protein named for its primary function, growth stimulation. If too little or too much GH is secreted, dwarfism or gigantism results. The critical maintenance of normal GH levels is the responsibility of a variety of other hormones. Strothers treats cells dispersed from a cow's pituitary gland with some of these regulating hormones and looks at the proteins consequently produced by the cells to see if different GH variants are affected.
Two techniques, gel electrophoresis and Western blotting, help Strothers find affected varieties of GH. Becoming adept at these techniques required a good deal of time, and even a little blood. Strothers recalls shattering an Erlenmeyer flask, cutting his hand in the process. "I felt clumsier than I had ever felt before," a feeling, he claims, that passes after a few months of experience.
A third undergraduate researcher, Deirdre Reardon '96 B.S. Chem, says that overcoming those initial insecurities is the biggest step in gaining confidence in a laboratory setting, a step she is glad to have taken before entering graduate school. "If you have to go through that step when everybody else is on the second round, and you are on your first, you'll be lost, absolutely lost," Reardon shakes her head and tucks a strand of long red hair behind her ear.
For ten semesters Reardon has worked with Gregory Farber on a computational biochemistry project. Although she was uncertain whether she'd like the research at first, it wasn't long, she says, before she was seduced by the ideas generated as the project progressed. "My project deals with these eight-stranded alpha/beta barrels," she says enthusiastically. She describes a large family of enzymes that share a common three-dimensional fold, called the eight-stranded alpha/beta barrel. But that is all they share. These enzymes do different things and are made up of different sequences of amino acids. Why then is the alpha/beta barrel structure seen again and again in such seemingly unrelated enzymes? A simple answer would be that the alpha/beta barrel fold is just very stable, but Reardon decides to look at things differently.
She explains that this common fold may find its roots in an extinct, or yet undiscovered, ancestral enzyme. The differences in amino acid sequences between the alpha/beta barrel enzymes could reflect the fact that they represent distant branches on the family tree. In order to understand these enzymes in an evolutionary light, more, and older, family members are needed. Reardon writes computer programs to search a database containing the sequence of every known protein for the missing links. This quest has been successful. Reardon and Farber published a review article on the alpha/beta barrel folding motif in the FASEB Journal while she was an undergraduate. She is now attending the University of California at Berkeley to earn a Ph.D. in Biochemistry.
Goller, Strothers, and Reardon all say that doing research has made their science courses more interesting, and therefore, easier. Penn State undergrads also typically earn independent-study credits for their research time and often are employed by their mentors during the summer. They warn that research takes a lot of time, but agree that the benefits of being immersed in a research setting are completely worth it. Goller feels that if he hadn't become involved in research at Penn State, he would have deprived himself of a big part of his education. "There are faculty members," he says, "who take in undergrads for the sake of teaching," a far deeper level of teaching than can be reached in the classroom alone.
This story was written by Amy J. Davis '96 B.S. Biol, shortly before she and the undergraduates she interviewed graduated from Penn State.