Principal research results are related to development and application of novel methods for studies of the spatial structure of proteins and peptides using optical spectroscopy and molecular modeling. The results were published in some 100 papers in peer-reviewed scientific journals.
1985—1992. A series of studies dealing with the development of new methods in resonance (RR) and surface-enhanced (SER) Raman scattering of peptides and proteins. SER spectra of two membrane proteins — bacterial and visual rhodopsins — were detected for the first time. Based on the spectral data and the results of quantum chemical calculations, topology of the chromophore-binding sites of the two proteins was investigated. For a number of membrane proteins, UV RR spectra were obtained for the first time. Efficient methods for digital processing of signals in RR spectra of proteins were elaborated.
1992-1997. A series of molecular modeling studies of the structure of transmembrane (TM) domain of Na,K-ATPase was carried out. Detailed mapping of the spatial hydrophobic/hydrophilic properties of TM helices was done for the first time using the concept of the molecular hydrophobicity potential (MHP) approach. The MHP-technique was also employed to assess hydrophobic organization of a number of water-soluble and membrane proteins and peptides.
1997—2001. An original theoretical model of implicit membrane was developed. The model is destined for simulations of proteins and peptides in membrane-mimic environment. Computational results obtained for a large number of transmembrane and peripheral peptides were shown to agree well with the experimental data.
2002–present. Development of state-of-the-art multiscale approaches in computational modeling of peptides and proteins in membranes of different composition and in water. Application of the approaches to study protein-protein, protein-membrane, and protein-ligand interactions. Employment of the developed techniques in investigation of peripheral and integral membrane proteins, membrane-active peptides, as well as in rational molecular design of novel biologically active compounds with predefined properties — acting on targets in cell membranes. Creation of the united informational/computational complex for high-throughput molecular modeling of proteins and peptides.