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Yvonne Gindt, assistant professor of chemistry, has received a three-year, $100,000 grant from the National Institutes of Health to continue her research with Lafayette students on protein folding and aggregation, processes linked to a wide range of diseases, including Alzheimer’s, Parkinson’s, diabetes mellitus, and emphysema.
Katie Thoren ’06 of Hebron, Conn., and biochemistry majors Steven Presciutti ’05 (Wilkes-Barre, Pa.) and Maura Scolere ’05 (Clarks Summit) are working with Gindt on the project this summer through Lafayette’s EXCEL Scholars program, in which students collaborate with faculty on research while earning a stipend. Lafayette is a national leader in undergraduate research. Many of the 180 students who participate in EXCEL each year go on to publish papers in scholarly journals and/or present their research at conferences.
Gindt investigated improper folding of proteins with three students who presented their findings last year at the Intercollegiate Student Chemists Convention in Annville, Pa.
They include Meghan Ramsey ’04 (Lakeville, Minn.), recipient of Lafayette’s Trustee Scholarship and the national Goldwater Scholarship, the premier undergraduate award in math, science, and engineering.
“This project was very exciting because proteins are essential components of organisms, including humans,” says Ramsey, a neuroscience major and varsity soccer standout. “If protein structure can be better understood, then it may open doors to understanding diseases that result from proteins that do not fold properly.”
Trustee Scholarship recipient Stacey Wagner ’03 (Shavertown, Pa.), who graduated cum laude May 24 with honors in biochemistry, used biochemistry and physical chemistry techniques to investigate protein isolation and stabilization. Her work included growing E. coli bacteria engineered to produce excess amounts of the protein being studied. The addition of a small molecule or inducer to the bacteria caused production of the protein, which she later analyzed.
“She used a combination of techniques and concepts covered in the classroom along with some specialized material that a student wouldn’t normally see until graduate school,” says Gindt, who advised Wagner on her honors thesis.
Wagner and Ramsey coauthored a paper with Gindt and other researchers that was presented last August at the annual meeting of the American Chemical Society in Boston, Mass., and published in its proceedings.
Wagner also was one of 23 Lafayette students to give presentations in March at the 17th annual National Conference on Undergraduate Research. A member of an Alternative School Break team that worked on home construction for low-income families in Budapest, Hungary, Wagner coauthored three published articles in scientific journals on other Lafayette research in less than two years. She is a member of Sigma Xi, the international honor society for scientific and engineering research.
Biochemistry major Katelyn Connell ’04 (Modena, N.Y.) examined protein folding mechanisms by treating a protein with a dye.
“The EXCEL research is a great opportunity to be exposed to different techniques,” she says. “It’s not like the classroom; it’s like nothing I’ve ever done before. It’s real hands-on experience.”
Connell, Wagner, Ramsey, Gindt and other researchers wrote a research paper presented last August at the 18th Annual Conference on Raman Spectroscopy in Budapest, Hungary, and published in its proceedings.
Gindt says her research is just starting to uncover the importance of protein folding and aggregation in a wide range of diseases.
“Chemical reactions in biological systems are controlled and catalyzed by large molecules called proteins,” she explains. “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. 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.”
The basic underlying forces that cause proteins to associate are not well understood, partially due to the challenges of studying such large molecules.
“We are still unsure about what steps must occur to either prevent or facilitate protein association,” says Gindt. “To study such processes, we have selected a model system with some unique features that allow us to follow the actual association steps.”
Most protein molecules are colorless to the human eye and do not absorb visible light. Gindt’s model system, phycocyanin, evolved in blue-green algae to specifically absorb visible light for photosynthesis.
“The protein contains a colored entity that is sensitive to both the folding state of the protein and its association state. Therefore, by monitoring the amount of visible light absorbed by the colored entity, we can determine if the protein molecule is in its proper shape and if the protein has associated with other proteins. Since we can monitor the amount of light absorbed with time, we are able to decipher the intermediates that form going from one state of the protein to another as we monitor the rate of these reactions. These experiments will allow us to learn more about the basic biochemistry that is involved when proteins associate in either favorable or unfavorable ways.”
Gindt, who regularly publishes her research in scientific journals, previously received grants from the National Science Foundation and Nebraska Foundation. She also has won National Merit, Krause (University of Wisconsin-Eau Claire), and American Chemical Society Scholarships.
Before becoming a member of the Lafayette faculty in fall 2001, Gindt had taught at the University of Nebraska at Kearney since 1995, serving her last year there as an associate professor with tenure. She earned a Ph.D. from the University of California, Berkeley, in 1993, and a B.S. from the University of Wisconsin-Eau Claire in 1988. She served as a post-doctoral research associate at Lawrence Berkeley Laboratory and Michigan State University.
Her research interests include biophysical chemistry, protein quaternary structure, and time-resolved spectroscopy.