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Piatok, 22. novembra 2024
The Nobel Prize in Chemistry
Dátum pridania: 21.08.2007 Oznámkuj: 12345
Autor referátu: holdenko
 
Jazyk: Angličtina Počet slov: 10 788
Referát vhodný pre: Gymnázium Počet A4: 37.9
Priemerná známka: 2.95 Rýchle čítanie: 63m 10s
Pomalé čítanie: 94m 45s
 

Several Nobel Prizes for Chemistry have been awarded for work in photosynthesis and respiration, the two main processes in the energy metabolism of living organisms (cf. Section 3.5). In 1961 Melvin Calvin of Berkeley received the prize for elucidating the carbon dioxide assimilation in plants. With the aid of carbon-14 (cf. Section 3.6) Calvin had shown that carbon dioxide is fixed in a cyclic process involving several enzymes. Peter Mitchell of the Glynn Research Laboratories in England was awarded in 1978 for his formulation of the chemiosmotic theory. According to this theory, electron transfer (cf. Sections 3.3 and 3.4) in the membrane-bound enzyme complexes in both respiration and photosynthesis, is coupled to proton translocation across the membranes, and the electrochemical gradient thus created is used to drive the synthesis of ATP (adenosine triphosphate), the energy storage molecule in all living cells. Paul D. Boyer of UCLA and John C. Walker of the MRC Laboratory in Cambridge shared one-half of the 1997 prize for their elucidation of the mechanism of ATP synthesis; the other half of the prize went to Jens C. Skou in Aarhus for the first discovery of an ion-transporting enzyme. Walker had determined the crystal structure of ATP synthase, and this structure confirmed a mechanism earlier proposed by Boyer, mainly on the basis of isotopic studies.
Luis F. Leloir from Buenos Aires was awarded in 1970 "for the discovery of sugar nucleotides and their role in the biosynthesis of carbohydrates". In particular, Leloir had elucidated the biosynthesis of glycogen, the chief sugar reserve in animals and many microorganisms. Two years later the prize went with one half to Christian B. Anfinsen of NIH and the other half shared by Stanford Moore and William H. Stein, both from Rockefeller University, for fundamental work in protein chemistry. Anfinsen had shown, with the enzyme ribonuclease, that the information for a protein assuming a specific three-dimensional structure is inherent in its amino-acid sequence, and this discovery was the starting point for studies of the mechanism of protein folding, one of the major areas of present-day biochemical research. Moore and Stein had determined the amino-acid sequence of ribonuclease, but they received the prize for discovering anomalous properties of functional groups in the enzyme's active site, which is a result of the protein fold.

Naturally a number of Nobel Prizes for Chemistry have been given for work in the nucleic acid field. In 1980 Paul Berg of Stanford received one half of the prize for studies of recombinant DNA, i.e. a molecule containing parts of DNA from different species, and the other half was shared by Walter Gilbert from Harvard and Frederick Sanger (see Section 3.5) for developing methods for the determination of the base sequences of nucleic acids. Berg's work provides the basis of genetic engineering, which has led to the large biotechnology industry. Base sequence determinations are essential steps in recombinant-DNA technology, which is the rationale for Gilbert and Sanger sharing the prize with Berg. Sidney Altman of Yale and Thomas R. Cech of the University of Colorado shared the prize in 1989 "for their discovery of the catalytic properties of RNA". The central dogma of molecular biology is: DNA –> RNA –> enzyme. The discovery that not only enzymes but also RNA possesses catalytic properties have led to new ideas about the origin of life. The 1993 prize was shared by Kary B. Mullis from La Jolla and Michael Smith from Vancouver, who both have given important contributions to DNA technology. Mullis developed the PCR ("polymerase chain reaction") technique, which makes it possible to replicate millions of times a specific DNA segment in a complicated genetic material. Smith's work forms the basis for site-directed mutagenesis, a technique by which it is possible to change a specific amino-acid in a protein and thereby illuminate its functional role.
 
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Zdroje: Westgren, A., Nobel – The Man and His Prizes, ed. Odelberg, W. (Elsevier, New York, 1972), pp. 279-385., Kormos Barkan, D., Walther Nernst and the Transition in Modern Physical Science, (Cambridge University Press, 1999)., Rife, P., Lise Meitner and the Dawn of the Nuclear Age, (Birkhäuser, 1999).
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