Olga Pakhomova received her M.S. in Microbiology from the Moscow State University and Ph.D. in Biophysics/Radiation Biology from Medical Radiology Research Center in Obninsk, Russia.
In 1997, she became a research fellow at Biochemistry Department of University of Texas Health Science Center at San Antonio (UTHSCSA) and studied interaction of ribosomal L5 protein and its cognate 5S RNA. Starting in 2000, she continued postdoctoral training at the Structural Biology Center of UTHSCSA and conducted studies on characterization of protein-nucleic acid and protein-protein interactions in solution. She determined and characterized a novel structure of an RNA-binding protein SRP19 by pulsed NMR spectroscopy. She also employed NMR and complementary methodologies (surface plasmon resonance, fluorescence methods, analytical ultracentrifugation, mass spectrometry) to analyze the molecule of betaglycan, a TGFb receptor, and to characterize its interaction with TGFb receptor ligands. Starting in 2005, she focused on protein structure determination by X-ray macromolecular crystallography. She resolved and described the molecular structure of an Cu/Zn superoxide dismutase from C. elegans. Mutations that alter function of a homologous enzyme in humans are associated with an inherited form of amyotrophic lateral sclerosis (ALS), a disease that manifests in progressive degeneration of motor neurons. Another accomplished project was structural and functional characterization of a toxic ADP-ribosyltransferase produced by M. pneumoniae , which is responsible for sequelae of M. pneumoniae infections in human.
In March 2009, she joined Frank Reidy Research Center for Bioelectrics at Old Dominion University as an Associate Research Professor, and is currently involved in the analysis of structure and function of lipid nanopores in the cell plasma membrane.