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For nearly 10 months, Marquis Scholar Katie Thoren ’06 (Hebron, Conn.) has carefully observed interactions between and among chains of amino acids, learning how the proteins they comprise fold and unfold. She presented the results of her work, which may help the effort to cure certain diseases, at the national meeting of the American Chemical Society, held March 28 to April 1 in Anaheim, Calif.
Thoren, a chemistry major and member of the crew club, is particularly interested in proteins that fold improperly, clumping together and forming masses. These kinds of proteins are found in the brains of people suffering from Alzheimer’s and Parkinson’s diseases, and researchers are hoping to learn more about them in an attempt to discover new therapies – or even cures – for these diseases.
“Researchers don’t know whether protein misfolding is the cause or result of diseases like Alzheimer’s,” Thoren says. “So basically, if we figure out how protein folding happens in general, maybe we can figure out the mechanisms of these diseases.”
Thoren’s research is part of a larger project on protein folding and aggregation led by Yvonne Gindt, assistant professor of chemistry, and funded by a three-year, $100,000 grant from the National Institutes of Health.
The two are working together through Lafayette’s distinctive EXCEL Scholars program, in which students assist faculty with research while earning a stipend. Lafayette is a national leader in undergraduate research. Many of the more than 160 students who participate in EXCEL each year go on to publish papers in scholarly journals and/or present their research at conferences.
“In many cases, the protein molecules must associate, or oligomerize, with other protein molecules to form an active complex that is actually responsible for carrying out the chemistry,” Gindt says. “For example, the structure that carries the oxygen in your blood, hemoglobin, is actually a complex of four proteins. In other cases, proteins that normally act alone in a biological system can associate in an undesirable way that causes problems for the biological system; Alzheimer’s disease appears to be an example of unfavorable protein association.”
Gindt says that Thoren was quick to grasp the complicated techniques needed for the research and, in less than a year, is able to understand the research process on a mature level.
“She recognizes when an experiment isn’t working,” Gindt says. “She kind of knows what to expect. That’s a very good trait in someone that young.”
Thoren, whose work also involves observing the groups of atoms that give color to protein molecules, uses a piece of equipment called a fluorimeter, acquired through the NIH grant, to excite the molecules with a specific wavelength of light. She points out that she feels fortunate to work so closely with Gindt, and to use sophisticated equipment in a well equipped, modern laboratory.
“If I had gone to a different school, I wouldn’t have had this opportunity,” she says.
Thoren plans to continue her work with Gindt over the summer, and possibly into her junior and senior years.
“I now see the bigger picture and there’s so much more I would like to learn about it,” she says. “I see how my research connects to bigger problems.”
Thoren, a graduate of Regional Hebron Andover Marlborough High School in Hebron, is a member of the College chapter of the American Chemical Society. She hopes to continue her studies in graduate school, possibly focusing on biological processes that relate to human health.
As a national leader in undergraduate research, Lafayette sends one of the largest contingents to the National Conference on Undergraduate Research each year. Forty-two students have been accepted to present their work at the annual conference this month.