Raquel Lieberman
Professor
Raquel Lieberman is the Sepcic-Pfeil Professor of Chemistry & Biochemistry at Georgia Tech. Her research program focuses on biophysical and structural characterization of proteins and the impact of disease-associated mutations on function or dysfunction (e.g. aggregation). Rooted in basic research, the long-term goal of her research program is to convert mechanistic discoveries into disease-modifying therapies.
A major research project in her lab is investigations of glaucoma-associated herocilin, which has been funded by NIH since March 2011. Her lab has made major strides toward detailed molecular understanding of herocilin structure, function, and disease pathogenesis. They have divulged similarities between herocilin-associated glaucoma and other protein misfolding disorders, particularly aherloid diseases. Cumulatively, their work is leading to the first disease-modifying glaucoma therapeutic.
Lieberman also has a track record in membrane enzymes dating back to her thesis work where she solved the first crystal structure of the copper-dependent particulate methane monooxygenase. During her postdoc she shifted focus to intramembrane aspartyl proteases (IAPs), particularly those involved in neurodegenerative disease like Alzheimer’s disease. In her independent lab she developed new proteomics-based assays to measure IAP proteolysis. The lab also collaborates with physicists at Oak Ridge National Labs to use neutron scattering to probe structure and lipids in solution. This work has been funded by NSF and NIH.
She serves on the Executive Council of the Protein Society and as an academic editor for PLoS Biology. She also serves as co-PI of the Department of Education GAANN program in Biochemistry & Biophysics at Georgia Tech and on the advisory committees in a variety of capacities.
raquel.lieberman@chemistry.gatech.edu
404-385-3663
Office Location:
Petit Biotechnology Building, Office 1308
The Lieberman research group focuses on biophysical and structural characterization of proteins involved in misfolding disorders. One major research project in the lab has been investigations of the glaucoma-associated myocilin protein. The lab has made major strides toward detailed molecular understanding of myocilin structure, function, and disease pathogenesis. Our research has clearly demonstrated similarities between myocilin glaucoma and other protein misfolding disorders, particularly amyloid diseases. The work has led to new efforts aimed at amelioratingthe misfolding phenotype using chemical biology approaches. Our second project involves the study of membrane-spanning proteolytic enzymes, which have been implicated disorders such as Alzheimer disease. Our group is tackling questions surrounding discrimination among and presentation of transmembrane substrates as well as the enzymatic details of peptide hydrolysis. In addition to the biochemical characterization of intramembrane aspartyl proteases, our group is developing new crystallographic tools to improve the likelihood of determining structures of similarly challenging membrane proteins more generally.
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