ИСТИНА

In recent decades, we witness a swift development of molecular biology and a large number of its related fields, such as biotechnology, immunology, molecular pharmacology, virology, etc. Success of the research in these fields is based on technological breakthrough, which made possible to establish both primary and three-dimensional structure of nucleic acids, proteins and other biological macromolecules. Biomolecular NMR spectroscopy is one of techniques that change the landscape of structural biology. Until recently NMR methods could deal only with a relatively small proteins or nucleic acids, with a molecular weight of about 10-15 kDa. Today, due to equipment enhancements, creation of novel NMR methodologies and use of isotopically enriched biomolecules it became possible to explore much larger objects – up to megadalton molecular weight. NMR methods provide with not only structural information, but also give insights into dynamic properties of biomolecules at atomic resolution. Unique capabilities of NMR spectroscopy to detect intermolecular interactions formed the basis for a new booming approach - NMR screening of biologically active compounds. As part of present lecture, we will examine modern approaches of signal assignment in biomolecules, methods to determine protein structure in solution, techniques to study protein dynamics in a large time scale - from picoseconds to hours. Novel approaches to study large biomolecules and NMR screening techniques will be discussed. Advantages and fundamental limitations of NMR spectroscopy to study biomolecules will also be examined, and progress in overcoming of such limitations will be reported.