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”.