Christopher Jaroniec, associate professor of chemistry, is clearly one of the country’s top young researchers in his field, but he is pleased that the Camille Dreyfus Teacher-Scholar Award does not acknowledge just his research program.

“It is certainly a big honor to be recognized for research achievements,” Jaroniec said, “but, equally important, also for the commitment to educating students—graduate and undergraduate, which is highly rewarding.

“On the practical level, I very much appreciate receiving an unrestricted five-year research grant. And, for me personally, it is a tremendous opportunity to be invited to join a community of teacher-scholars. This will provide possibilities to discuss research as well as novel approaches to education, which can give numerous new ideas that enhance one’s own teaching methods,“ Jaroniec said.

In the Jaroniec laboratory, which right now includes three postdoctoral researchers and nine graduate students—Jaroniec frequently has a cadre of undergraduate students and sometimes high-school students as well--work involves developing ways to get a better look at the structure and dynamics of large biological molecules that defy analysis by conventional tools of structural biology, X-ray crystallography and solution state nuclear magnetic resonance (NMR) spectroscopy.

Instead, Jaroniec and other researchers in this area rely on solid state NMR spectroscopy to detect the arrangements of atoms in proteins, but translating solid state NMR data into actual 3D protein structures can be difficult. 

Recently, Jaroniec and his colleagues found a new method that better reveals the structure of proteins. Being able to “see” the structure is critical in allowing researchers to understand the function and interaction of biological molecules —both those involved in causing disease and those performing critical functions in healthy cells. This new solid state NMR method uses paramagnetic tags to help visualize the shape of protein molecules.

The importance of the ability to see the structures of complex protein assemblies is apparent when one realizes such protein systems include amyloids–fibrous clusters of proteins found in diseased cells that are associated with the development of certain neurological diseases in humans, many of which are incurable and ultimately fatal. Jaroniec is one of many researchers worldwide working to understand how these types of proteins cause degenerative brain and other diseases at the molecular level.

In fact, in 2008, Jaroniec was one of the first to take an atomic-level look at a protein that causes hereditary cerebral amyloid angiopathy (CAA)—a disease thought to cause stroke and dementia. He and his co-workers were able to use sophisticated solid state NMR methods to pinpoint a tiny portion of the protein molecule key to forming plaques in blood vessels in the brain.

In addition to this year’s Camille Dreyfus Teacher-Scholar Award, Jaroniec previously received a CAREER award from the National Science Foundation, an Eli Lilly Young Investigator Award in Analytical Chemistry, and a New Investigator Research Grant Award from the Alzheimer’s Association. His research is currently supported by the National Science Foundation, the National Institutes of Health, the Camille & Henry Dreyfus Foundation, and Eli Lilly.