Eighth Shull Fellow to Focus on Biochemistry and CrystallographyKatie Elyce Jones
February 07, 2014
Clifford G. Shull Fellowship recipient Mayank Aggarwal.
Biochemist and molecular biologist Mayank Aggarwal has been awarded this year’s Clifford G. Shull Fellowship. Aggarwal is the eighth fellow to join the Neutron Sciences Directorate at Oak Ridge National Laboratory since the program began in 2006. Named for the 1994 Nobel Prize winner in Physics who did his early neutron scattering research at Oak Ridge from 1946 to 1955, the Shull fellowship program recruits outstanding early-career researchers who use neutrons in their field of science or engineering.
During his doctoral research, Aggarwal used neutron and x-ray crystallography to study the structure and function of carbonic anhydrase (CA), a protein found in humans. CA uses hydrogen atoms to aid conversion of carbon dioxide into carbonic acid, a chemical reaction essential to many bodily functions. A number of slightly different forms of CA are found in humans. The forms Aggarwal studies are targets for drug design research aimed at creating better CA inhibitors, a class of drugs that interrupts the reactions caused by CA and improves management of conditions such as glaucoma, epilepsy, and even cancer.
“My goal at ORNL is to solve various neutron structures of human CA,” Aggarwal said. “This could help in developing a database of better and more specific inhibitors for human CAs.”
Like Shull—who considered the hydrogen structure in crystals a crucial area of study in neutron scattering—Aggarwal uses neutrons to locate the exact position of hydrogen atoms in proteins making up CA enzymes.
“We cannot visualize hydrogen atoms in a protein structure with x-ray crystallography, but neutron diffraction is able to offer that information,” Aggarwal said.
Aggarwal received his PhD in biochemistry and molecular biology from the University of Florida, and his work has appeared in 16 journal publications, including Journal of the American Chemical Society, Biochemistry, and Acta Chrystallographica Section D: Biological Crystallography.