Tag Archives: proteins

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”.

Scientific investigations of the Nobel prize winner Emil Fischer as a launching pad for the development of biochemistry: a brief overview

T. V. Danylova1, S. V. Komisarenko2

1National University of Life and Environmental Sciences of Ukraine, Kyiv;
e-mail: danilova_tv@ukr.net;
2Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: svk@biochem.kiev.ua

Modern biochemistry and molecular biology would be impossible without discoveries in related fields of science. This paper aims to outline briefly the main stages of scientific activity of a Nobel Prize winner 1902 – German chemist Hermann Emil Fischer, one of the leading chemists of all times. Emil Fischer was a brilliant multifaceted scientist who left his mark in organic chemistry, physiology, medicine, gave impetus to the development of biochemistry. His insights into the structures of sugars, enzymes, proteins, and purines have become a launching pad for the further development of biochemistry and molecular biology. His contribution to the natural sciences was immense; some chemical reactions and concepts were named after him. This prominent scientist was honored with a number of awards.

Modification of spectrophotometric method of determination of protein carbonyl groups

O. V. Zaytseva, S. G. Shandrenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: Olgga__89@mail.ru

Basing on detailed study of optical absorption spectra of protein-hydrazones a modification of the spectrophotometric method determination of the protein carbonyl groups has been proposed. For the hydrazone adduct determination we proposed to measure the optical absorption at three wavelengths (320, 370 and 420 nm) instead of only one (at 370 nm). Two additional wavelengths are used for the linear approximation of the background optical spectrum. This modification improves the specificity and reduces the error when determining the content of CO groups in proteins.

Legume-rhizobium symbiosis proteomics: achievements and perspectives

Iu. Iu. Kondratiuk, P. M. Mamenko, S. Ya. Kots

Institute of Plant Physiology and Genetics, National Academy of Sciences of Ukraine, Kyiv;
e-mail: kondratyuk_yulya@ukr.net

The present review contains results of proteo­mic­ researches of legume-rhizobium symbiosis. The technical difficulties associated with the methods of obtaining protein extracts from symbiotic structures and ways of overcoming them were discussed. The changes of protein synthesis under formation and functioning of symbiotic structures were shown.  Special attention has been given to the importance of proteomic studies of plant-microbe structures in the formation of adaptation strategies under adverse environmental conditions. The technical and conceptual perspectives of legume-rhizobium symbiosis proteomics were shown.