Amino Acids, Proteins and Cancer Biochemistry by Jesse P. Greenstein, John T. Edsall

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By Jesse P. Greenstein, John T. Edsall

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1955; Tanford and Hauenstein, 1956). Attempts were, therefore, made to render the tyrosyl and carboxyl groups normal with the aid of a hydrogenbond-breaking, or denaturing, solvent. For this purpose a study of hydrogen ion equilibria of ribonuclease in a denaturing solvent was carried out (Cha and Scheraga, 1960). A similar investigation had previously been carried out by Blumenfeld and Levy (1958) for the tyrosyl groups. 2 M in urea (designated as GU). , 1959). By this choice of solvent it was possible to avoid large solvent effects on the pK's.

The hydrogens may thus be grouped in four sets of 175, 25, 25, and 20 each. The 70 hydrogens of the last three sets are considered to be involved in hydrogen bonding of different bond strengths, the last set of 20 presumably being most tightly bound. In view of the discrepancy in the number of rapidly exchangeable hydrogens (175 compared with 160), cited earlier,3 the first set of 25 could be a larger set, possibly as large as 40. This would mean that the total number of hydrogen bonds could be as high as 85.

Chem. Soc, Chicago, Illinois, Sept. 1958, p . 51C. Scheraga, H . A. (1959). Ann. Rev. Phys. Chem. 10,191. Scheraga, H . A. (1960). J. Am. Chem. Soc, in press. Scheraga, H . , and Mandelkern, L. (1953). J. Am. Chem. Soc. 75, 179. Schildkraut, C. , and Scheraga, H . A. (1960). J. Am. Chem. Soc. 82, 58. , and Anfinsen, C. B. (1957). Biochim. et Biophys. Acta 24, 229. , Anfinsen, C. , and Harrington, W . F . (1957). Biochim. et Biophys. Acta 26, 502. Shugar, D . (1952). Biochem. J. 52, 142. Spackman, D .

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