Research interests focused on application of spectroscopy, especially electron paramagnetic resonance (EPR) and fluorescence, in chemistry and biology, specifically to study structure and dynamics of membranes and proteins, drug-protein, and protein-protein interactions.

• Site-directed spin labeling of proteins: measuring protein distances in solution, protein folding/unfolding; interactions of protein with drugs and environment; docking of fatty acids and drug molecules in lipophilic protein channels.
• Dynamics of lipids and lipid-protein interactions.
• Pico-to-nanosecond dynamics of small molecules in complex systems.
• Characterization of transient free radicals by spin trapping EPR.
• Electron spin exchange and dipolar interactions in liquids and low-dimensional magnetic systems including metallo-organic ferromagnets: theoretical and experimental aspects.
• Magnetic susceptibility and EPR studies of low-dimensional systems.

Current project focuses on understanding molecular aspects of binding and interactions of MRI paramagnetic contrast agents (PCA) molecules with several key biomolecules, such as blood pool proteins and phospholipids, and the relationship between structure of PCA’s and their binding properties and proton relaxation enhancement. The goal will be achieved by investigating these interactions and their effects on structure and electronic properties of PCAs' by variety of spectroscopic techniques, including fluorescence, NMR, and EPR at multiple frequencies.