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Quantum Yields for Photolysis of the Peptide Bond at 2537 A.

Abstract

FROM a study of the action of ultra-violet light on monolayers of proteins, Mitchell1 suggested that tyrosine absorption leads to breakage of the —CONH— bond adjacent to the chromophore. According to Pauling and Niemann2 the C—N linkage has the lowest bond energy and should, therefore, be the first to break when energy is supplied to the molecule. Mitchell's model experiments for proteins with stearyl anilide suffer from the drawback that the phenyl group is directly adjacent to the —CONH— link, but Carpenter3 has shown that, with benzyl stearyl amine and β-phenyl ethyl stearyl amine, cleavage also occurs where the benzene ring and the —CONH— linkage are separated by one or two —CH2— groups.

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References

  1. Mitchell, J. S., Proc. Roy. Soc., A, 155, 696 (1936); Nature, 137, 509 (1936).

    CAS  Google Scholar 

  2. Pauling, L., and Niemann, C., J. Amer. Chem. Soc., 61, 1860 (1939). See also Rideal, E. K., and Mitchell, J. S., Proc. Roy. Soc., A, 159, 206 (1937).

    Article  CAS  Google Scholar 

  3. Carpenter, D. C., J. Amer. Chem. Soc., 62, 289 (1940).

    Article  CAS  Google Scholar 

  4. Van Slyke, D. D., Dillon, R. T., MacFayden, D. A., and Hamilton P., J. Biol. Chem., 141, 627, 671 (1941).

    CAS  Google Scholar 

  5. Carpenter, D. C., J. Franklin Inst., 232, 76 (1941).

    Article  CAS  Google Scholar 

  6. Abderhalden, E., and Haas, R., Z. physiol. Chem., 155, 202 (1926). Eckstein, H. C., and Lieben, F., Biochem. Z., 263, 366 (1933). Rao, G. G., and Dhar, N. R., J. Ind. Chem. Soc., 11, 617 (1934). Guillaume, A., and Tanret, G., C.R. Acad. Sci., Paris, 201, 1057 (1935); Bull. soc. chim. biol., 18, 556 (1936).

    Google Scholar 

  7. Weizmann, C., Hirshberg, Y., and Bergmann, E., J. Amer. Chem. Soc., 60, 1799 (1938).

    Article  CAS  Google Scholar 

  8. Allen, A. J., Steiger, R. E., Magill, M. A., and Franklin, R. G., Biochem. J., 31, 195 (1937).

    Article  CAS  Google Scholar 

  9. Levy, B., M.S. Thesis, Polytechnic Inst., Brooklyn (1948).

  10. McLaren, A. D., and Pearson, S., J. Polymer Sci., 4, 45 (1949).

    Article  ADS  CAS  Google Scholar 

  11. McLaren, A. D., in “Advances in Enzymology’ (Interscience, N.Y., vol. 9, in the press).

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MANDL, I., MCLAREN, A. Quantum Yields for Photolysis of the Peptide Bond at 2537 A.. Nature 164, 749–750 (1949). https://doi.org/10.1038/164749b0

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