Tag Archives: structure
The contribution of Nobel prize laureates to research of the protein structure: J. Sumner, J. Northrop, W. Stanley, L. Pauling, F. Sanger, M. Perutz, J. Kendrew
V. M. Danilova, R. P. Vynogradova, S. V. Komisarenko
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: valdan@biochem.kiev.ua
Received: 11 Match 2020; Accepted: 15 May 2020
The second half of the 20th century was marked by remarkable discoveries in the chemistry and biochemistry of proteins, in particular, in establishing the protein structure. James Sumner, John Northrop, and Wendell Stanley, the Nobel Laureates in chemistry in 1946, were the first to isolate individual enzymes and viruses in a pure crystalline form and prove their protein nature, thereby making an invaluable scientific contribution to the development of important biological disciplines such as biochemistry, enzymology, virology, and molecular biology. A significant contribution to understanding chemical bonding in the formation of the different levels of a protein structure was made by Linus Pauling – a prominent American scientist of the 20th century. He was awarded the Nobel Prize in Chemistry in 1954 “for his research into the nature of the chemical bond and its application to the elucidation of the structure of complex substances”. Biochemists know him well as the author of the secondary structure of proteins – the α-helix and the β-sheet. Frederick Sanger, a two-time Nobel Prize winner (1958 and 1980), was the first among researchers who determined the primary amino acid sequence of a protein, for example, of two insulin polypeptide chains A and B. F. Sanger proved that the sequence nature of proteins’ structures is analogous to that of gene sequences in the DNA, and thus, the same principles may be applied. The difficult question of how a protein molecule is arranged in space was answered by the English biochemists Max F. Perutz and John C. Kendrew. They determined the three-dimensional structure of hemoglobin and myoglobin proteins by X-ray diffraction and were awarded the Nobel Prize in Chemistry in 1962 “for their studies of the structures of globular proteins”.
Lipoxygenases and their metabolites in formation of plant stress tolerance
L. M. Babenko1, M. M. Shcherbatiuk1, T. D. Skaterna2, I. V. Kosakivska1
1M.G. Kholodny Institute of Botany, National Academy of Sciences of Ukraine, Kyiv;
2Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: lilia.babenko@gmail.com
The review focuses on the analysis of new information concerning molecular enzymology of lipoxygenases – proteins involved in lipid peroxidation and found in animals and plants. Modern concept of structural features, catalytic characteristics and functions of lipoxygenase family enzymes as well as products of their catalytic activity in plants have been discussed and summarized. Issues of enzyme localization in plant cells and tissues, evolution and distribution of lipoxygenases, involvement in production of signaling substances involved in formation of adaptation response to abiotic and biotic stress factors and in regulation of lipoxygenase signal system activity are highlighted. Participants of the elements signaling of LOX-pathway reception and transduction into genome are considered. Special attention is given to jasmonates, metabolites of the allene oxide synthase branch of the lipoxygenase cascade, because these metabolites have high biological activity, are ubiquitously present in all plant organisms, and are involved in regulation of vitally important processes. Data concerning lipoxygenase phylogeny, possible occurrence of a common predecessor for modern isoforms of the enzyme in pro- and eukaryote have been examined. Some results of our studies that open up possibilities of using the lipoxygenase catalytic activity characteristics as biological markers in plant stress tolerance researches are given.
Structure and functions of glutathione transferases
O. M. Fedets
Stepan Gzhytskyi Lviv National University of Veterinary Medicine and Biotechnologies, Ukraine;
e-mail: olehfedets@gmail.com
Data about classification, nomenclature, structure, substrate specificity and role of many glutathione transferase’s isoenzymes in cell functions have been summarised. The enzyme has been discovered more than 50 years ago. This family of proteins is updated continuously. It has very different composition and will have demand for system analysis for many years.