Raquel Lieberman is the Sepcic-Pfeil Professor of Chemistry and Biochemistry at Georgia Tech. Her research program focuses on the biophysical and structural characterization of proteins and on understanding how disease-associated mutations affect protein function or dysfunction (e.g., aggregation). Rooted in basic research, the long-term goal of her work is to translate mechanistic discoveries into disease-modifying therapies.

One major focus of her research is glaucoma-associated myocilin, a project that has been funded by the NIH since March 2011. Her lab has made significant progress toward a detailed molecular understanding of myocilin structure, function, and disease pathogenesis. This work has revealed similarities between myocilin-associated glaucoma and other protein misfolding disorders, particularly amyloid diseases. Collectively, these efforts are paving the way toward the first disease-modifying therapeutic for glaucoma.

Lieberman also has extensive experience in the study of membrane enzymes. During her thesis work, she solved the first crystal structure of the copper-dependent particulate methane monooxygenase. As a postdoctoral researcher, she shifted her focus to intramembrane aspartyl proteases (IAPs), particularly those involved in neurodegenerative diseases such as Alzheimer’s disease. In her independent laboratory, she developed new proteomics-based assays to measure IAP proteolysis. Her lab also collaborates with physicists at Oak Ridge National Laboratory to use neutron scattering to probe protein structure and lipids in solution. This work has been funded by both the NSF and NIH.

In addition to her research activities, Lieberman serves on the Executive Council of the Protein Society and as an academic editor for PLoS Biology. She is also co-PI of the Department of Education GAANN program in Biochemistry and Biophysics at Georgia Tech and serves on a variety of advisory committees.