Membrane is one of the main components of a living cell. It is involved in a variety of vital processes, including respiration, transport of nutrients, signaling, and enzymatic reactions. Integral and peripheral membrane proteins, such as receptors, transporters, ion channels, various enzymes that are directly involved in maintaining cell homeostasis and their reception of external and intercellular signals, are responsible for most of these functions. Up to 30% of all protein sequences encoded in the genomes of various organisms correspond to membrane proteins, and many socially significant diseases are associated with their dysfunction and mutations. Moreover, over half of currently known drugs directly affect the activity of membrane proteins. Therefore, it is not surprising that membrane proteins are among the most important objects for the pharmacological development of modern "targeted" drugs and early diagnostics. At the same time, membrane proteins are rather poorly studied from the point of view of the spatial structure, dynamics and intermolecular interactions, which is caused by technical problems associated with the heterogeneity of the membrane environment, their dimerization/oligomerization and the presence of disordered parts, causing a high relative mobility of subdomains. Directed design of biologically active compounds requires a deep understanding of the structural and dynamic organization and functioning of their protein targets that in many cases are localized inside or on the surface of biological membranes. The main achievements in this area are provided by X-ray crystallography and are presented by the studies of porins, ion channels, G-protein coupled receptors, as well as individual (including water-soluble) domains of membrane proteins. However, crystallization of membrane proteins leads to the loss of information on conformational mobility and makes it impossible to study the influence of the membrane environment on their structure, dynamics, and function. The fast-developing method of Cryo-Electron Microscopy allows obtaining the structure of full-length proteins and their complexes, including membrane proteins with a sufficiently high resolution. However, this method also has its own limitations when working with membrane proteins with high intramolecular motility (such as type I receptors with extracellular and cytoplasmic globular domains connected by flexible loops to transmembrane segment). Moreover, now there is no modern experimental base in Russia to use this method. Thus, both structural methods mentioned above should be combined with other methods of structural biology, allowing obtaining detailed experimental structural and dynamic information for proteins. Therefore, the development of new complex techniques for structural-dynamic studies based on the integration of complementary experimental and theoretical (computational) methods of structural biology, such as NMR spectroscopy, protein engineering, optical spectroscopy and computer modeling, is a modern trend contributing to obtaining unique data on the link between structure and function of membrane and membrane-active proteins. Heteronuclear NMR spectroscopy is a unique method that allows one to obtain experimental information about the structure, dynamics, and intermolecular interactions for peptides and proteins that often contain mobile segments and perform the biological function in a heterogeneous environment. Modern methods of protein engineering allow obtaining samples of membrane proteins and their fragments (including isotope-labeled derivatives) from various biological systems in sufficient quantities for structural studies. Using optical microscopy and spectroscopy it is possible to characterize protein samples, as well as to obtain experimental information about intermolecular interactions and structural and functional properties of protein compounds at the molecular and cellular levels. Computer modeling helps to investigate at the atomic level the structure and dynamics of proteins and membranes, to reveal their interactions when performing a biological function. The complexity of the project is also provided by the choice of objects that belong to different protein families and performing different functions. This will allow to establish general fundamental principles of biological activity, as well as to identify unique molecular mechanisms for membrane proteins from different families. At the same time, the study of a set of objects, that sufficiently cover a wide range of biological functions, has more chances for the successful development of new ligand molecules to membrane proteins. Thus, the fundamental knowledge about the structure-dynamics-function relationship for membrane proteins of various families obtained as a result of this project will be most successfully used to create pharmacological compounds with a given specificity and targeted delivery to certain membrane systems for adequate therapy and early diagnosis of socially significant diseases.