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

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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

机译：诺贝尔奖奖酶对蛋白质结构研究的贡献：J. Sumner，J. Northrop，W. Stanley，L.Pauling，F. Sanger，M. Perutz，J. Kendrew

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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”.

机译：20世纪下半叶是由蛋白质化学和生物化学的显着发现，特别是在建立蛋白质结构方面。 James Sumner，John Northrop和Wendell Stanley于1946年在化学中的诺贝尔·斯坦利，是第一个将个体酶和病毒以纯的结晶形式分离并证明他们的蛋白质，从而为重要生物学的发展做出了宝贵的科学贡献生物化学，酶学，病毒学和分子生物学等学科。在Linus Pauling制造了在形成不同水平的蛋白质结构中形成化学键的重要贡献 - 这是20世纪的着名美国科学家。他于1954年被授予诺贝尔化学奖，1954年“研究了化学键的性质及其在阐明了复杂物质结构的应用”。生物化学家认识他作为蛋白质二级结构的作者 - α-螺旋和β-薄片。弗雷德里克桑杰是一家双重诺贝尔奖获奖者（1958年和1980年），是研究人员中的第一个，例如，确定蛋白质的主要氨基酸序列A和BF Sanger证明了序列性质蛋白质结构类似于DNA中的基因序列的结构，因此可以应用相同的原理。难题如何在空间中排列蛋白质分子的难题是由英国生物化学家Max F. Perutz和John C. Kendrew回答。它们确定了X射线衍射血红蛋白和肌红蛋白蛋白的三维结构，并于1962年在1962年颁发了诺贝尔化学奖“，以他们对球状蛋白质结构的研究”。

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《Ukrainian Biochemical Journal》 |2020年第4期|共27页
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V. M. Danilova; R. P. Vynogradova; S. V. Komisarenko;
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F. SangerhemoglobininsulinJ. KendrewJ. NorthropJ. SumnerL. PaulingM. Perutzmyoglobinpepsinproteinsstructuretobacco mosaic virustrypsinureaseW. Stanleyα-helixβ-structure;

机译：F. sangerhemoglobininsulinj。 Kendrewj。诺罗特罗Sumnerl。保罗明。 Perutzmyoglobinpepsinproteinsstructuretobacco Mosaic Virustrypsinueasew。斯坦利α-螺旋β结构;

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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

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