Center for Proteomics and Bioinformatics:
|1987-1993||M.S., Medical Biochemistry, Moscow State Medical University, Russia|
|1993-1997||Ph.D., Biochemistry, Institute of Biomedical Chemistry, Moscow, Russia|
|1997-2003||Post-Doc, Proteins & Mass Spectrometry, Albert Einstein College of Medicine, Bronx, NY|
|2004-2005||Associate, Proteins & Mass Spectrometry, Albert Einstein College of Medicine, Bronx, NY|
|2005-||Instructor, Center for Proteomics & Bioinformatics, Case Western Reserve University, Cleveland, OH|
|1995-1996||J. Soros award for the best Scientist.s research. Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, Russia|
|1997-||American Society of Mass Spectrometry|
|2005||Second best poster, awarded with the free registration for the 8th International meeting on mass Spectrometry in the Health and Life Sciences|
1. Development of a new sensitive quantitative approach (SRM) for protein footprinting in order to improve detection and quantitation of oxidized products that are present in less then 1% of the unmodified peptide and remained undetected in the current analysis. Hydroxyl radical-mediated protein footprinting in combination with mass spectrometry has recently been developed to define protein structure, protein folding, and protein-protein and protein-DNA interactions in solution. This method is based on the measurement of the reactivity of amino acid side-chain groups with hydroxyl radicals resulting in covalent modification (oxidation) of these residues according to their solvent accessibility. Digested protein then analyzed by mass spectrometry for the sites of oxidation.
2. Developing and implementing new mass spectrometry based approaches for examining the post-translational modifications of proteins. Post-translational modifications (PTMs) are covalent modification of the proteins after its translation. PTMs have been shown to be important features for regulating protein functions, determining their activity state, cellular location and dynamic interaction with other proteins. Because they are present in substoichiometric amounts on protein molecules, the comprehensive analysis has some analytical limitations.