Ukr.Biochem.J. 2020; Volume 92, Issue 4, Jul-Aug, pp. 127-153


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;

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”.

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  1. Danylova TV, Komisarenko SV. Scientific investigations of the Nobel prize winner Emil Fischer as a launching pad for the development of biochemistry: a brief overview. Ukr Biochem J. 2018; 90(4): 135-142.  CrossRef
  2. Danilova VM, Vynogradova RP, Komisarenko SV. The contribution of the Nobel Prize laureates to the development of dynamic biochemistry and bioenergetics. E. Buchner, A. Kossel, R. Willstätter, O. Meyerhof, A. Hill, O. Warburg, A. Szent-Györgyi. Ukr Biochem J. 2019; 91(1):108-126.  CrossRef
  3. Vynogradova RP, Danilova VM, Komisarenko SV. The Nobel laureates’ contributions to the study of carbohydrate metabolism and its regulation. A. Harden, H. Euler-Chelpin, C. F. Cori, G. T. Cori, E. Sutherland, L. F. Leloir, H. Krebs, F. Lipmann, P. Mitchell. Ukr Biochem J. 2020; 92(1): 135-163. CrossRef
  4. Sumner James Batcheller. Nobel Prize Laureates: Encyclopedia: M-Ya: Trans. from English. M.: Progress, 1992. P. 351-354.
  5. Sumner James Batcheller. Regime of access :
  6. Regime of access :
  7. Leonard A.Maynard. James Batcheller Sumner. 1887-1955. National Academy of sciences, Washinton. 1958
  8. Regime of access :
  9. Nortrop John Howard. Nobel Prize Laureates: Encyclopedia: M-Ya: Trans. from English. M.: Progress, 1992. P. 165-166.
  10. John H. Northrop. Regime of access :
  11. Herriott RM. John Howard Northrop. National Academy of Sciences. 1994. Biographical Memoirs: V.63. Washington, DC: The National Academies Press. CrossRef
  12. Northrop JH. Crystalline pepsin. Science. 1929; 69(1796): 580.  PubMed, CrossRef
  13. Northrop JH. Crystalline pepsin : I. Isolation and test purity. J Gen Physiol. 1930; 13(6): 739-766. PubMed, PubMedCentral,CrossRef
  14. Northrop JH. Crystalline pepsin : II. General properties and experimental methods. J Gen Physiol. 1930; 13(6): 767-780. PubMed, PubMedCentral,CrossRef
  15. Northrop JH, Kunitz M. Crystalline trypsin : I. Isolation and tests of purity. J Gen Physiol. 1932; 16(2): 267-294. PubMed, PubMedCentral, CrossRef
  16. Northrop JH, Kunitz M. Isolation of protein crystals possessing tryptic activity. Science. 1931; 73(1888): 262-263. PubMed, CrossRef
  17. Vynogradova RP, Danilova VM, Komisarenko SV. Development on knowledge of hormone biochemistry in the works of the Nobel prize laureates of the first half of the 20th century: F. G. Banting, John J. R. Macleod, H. O. Wieland, A. O. Windaus, A. F. Butenandt, L. Ružička, E.Kendall, P. Hench, T. Reichstein. Ukr Biochem J. 2019; 91(3): 107-126. CrossRef
  18. Regime of access : mosaic virus.
  19. Wendell Meredith Stanley. Nobel Prize Laureates: Encyclopedia: M-Ya: Trans. from English. M.: Progress, 1992. P. 452-454.
  20. Regime of access :
  21. Regime of access :
  22. Wendell M. Stanley. Regime of access :
  23. Schachman HK, Ballou CE, Arhur Knight C. Wendell Meredith Stanley, Molecular Biology; Biochemistry: Berkeley. University of California: in Memoriam, 1974, p. 95-97, Academic Senate-Berkeley-Division.
  24. Colvig R. Wendell M. Stanley, PhD, (1905-1971). Cancer. 1972; 29(2): 541-542.   PubMed, CrossRef
  25. Wendell M.Stanley. The isolation and properties of crystalline tobacco mosaic virus. Nobel Lecture, December 12, 1946.
  26.  Regime of access :,Northrop,Stanley.html.
  27. Danylova T.V., Komisarenko S.V. Nobel prize Winner Erwin Schrödinger: The physicist, philosopher, and godfather of molecular biology and genetics. Ukr Biochem J. 2020; 92(3): 93-100.  CrossRef
  28. Alpha helix. Regime of access :
  29. Secondary catalase structure. Regime of access :
  30. Pouling Linus Carl. Nobel Prize Laureates: Encyclopedia: M-Ya: Trans. from English. M.: Progress, 1992. P. 232-237.
  31. Kakhovsky L. The 20th century chemist. Himia i zhizn. 1995; (7): 8-15.
  32. Linus Pouling – the greatest chemist of the 20th century (to the 100th birthday anniversary). Regime of access :
  33. Pouling Linus.  Regime of access :
  34. Regime of access :
  35. Linus Pauling. X-ray crystallography and the nature of the chemical bond. Oregon State University’s Special Collection, April 1991. Regime of access :
  36. Ridgway D. Interview with Linus Pauling. J Chem Educ. 1976; 53(8): 471-476. CrossRef
  37. Linus Pouling. The last interview. 1994 The Institute for Optimum Nutrition. Regime of access :
  38. Grigorieva MV, Danilova VM, Komisarenko SV. Brownian motion, electrophoresis, chromatography, and macromolecular chemistry: how it all unites Nobel laureates of the first half of the 20th century – T. Svedberg, A. Tiselius, R. Synge and H. Staudinger. Ukr Biochem J. 2019; 91(5): 70-79. CrossRef
  39. Regime of access :
  40. Sanger F, Nicklen S, Coulson AR. DNA Sequencing With Chain-Terminating Inhibitors. Proc Natl Acad Sci USA. 1977; 74(12): 5463-5467. PubMed, PubMedCentral, CrossRef
  41. Frederick Sanger. Nobel Prize Laureates: Encyclopedia: M-Ya: Trans. from English. M.: Progress, 1992. P. 379-383.
  42. Regime of access : Sanger.
  43. Regime of access :
  44. Regime of access :
  45. Levytsky EL. Frederick Senger is one of the founders of modern biotechnology. Biotechnology. 2008; 1(1): 123-125.
  46. Regime of access : proteins.
  47. Max Ferdinand Perutz. Nobel Prize Laureates: Encyclopedia: M-Ya: Trans. from English. M.: Progress, 1992. P. 214-216.
  48. Regime of access : Perutz.
  49. Regime of access :
  50. Regime of access : Maks Ferdinand.html
  51. Regime of access :
  52. Kendrew John Cowdery.  Nobel Prize Laureates: Encyclopedia: A-L: Trans. from English. M.: Progress, 1992. P. 541-543.
  53. Regime of access : Kendrew.
  54. Kendrew John. Regime of access : https://uk/
  55. Regime of access : Kendrew.html.

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