Chemistry of Natural Compounds

, Volume 12, Issue 3, pp 323–328 | Cite as

An investigation of the conformational states of the methylamide of N-acetyl-L-histidine

  • P. Berlin
  • M. Kreisler
  • S. F. Arkhipova
  • G. M. Lipkind
  • E. M. Popov
Article

Summary

1. All the conformational states of the methylamide of N-acetyl-L-histidine have been calculated.

2. It has been shown that in the case of the tautomer of the imidazole ring with a hydrogen atom on the\({\text{N}}^{\varepsilon _2 }\) atom, form R of the main chain is preferred, and in the tautomer with the proton on\({\text{N}}^\delta _1\) and also in the protonated state of the side chain B forms are preferred.

3. The conformational equilibrium is displaced in the direction of form I.

Keywords

Main Chain Imidazole Ring Conformational State Methylamide Nonvalent Interaction 

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Literature cited

  1. 1.
    E. M. Popov and G. M. Lipkind, Molekul. Biol.,5, 624 (1971).Google Scholar
  2. 2.
    G. M. Lipkind and E. M. Popov, Molekul. Biol.,5, 667 (1971).Google Scholar
  3. 3.
    E. M. Popov, G. M. Lipkind, S. F. Arkhipova, and V. G. Dashevskii, Molekul. Biol.,2, 612 (1968).Google Scholar
  4. 4.
    G. M. Lipkind, S. F. Arkhipova, and E. M. Popov, Izv. Akad. Nauk SSSR, Ser. Khim., No. 2, 315 (1970).Google Scholar
  5. 5.
    M. A. Kreissler, G. M. Lipkind, S. F. Arkhipova, and E. M. Popov, J. Chim. Phys., 913 (1974).Google Scholar
  6. 6.
    G. M. Lipkind and E. M. Popov, Int. J. Peptide Protein Res.,5, 371 (1973).CrossRefGoogle Scholar
  7. 7.
    G. M. Lipkind, S. F. Arkhipova, and E. M. Popov, Int. J. Peptide Protein Res.,5, 381 (1973).CrossRefGoogle Scholar
  8. 8.
    C. Long, Biochemists' Handbook, London (1961).Google Scholar
  9. 9.
    Biochim. Biophys. Acta,229, 1 (1971).Google Scholar
  10. 10.
    L. Pauling, The Nature of the Chemical Bond, third ed., Cornell Univ. Press, New York (1960).Google Scholar
  11. 11.
    M. S. Lehman, T. F. Koetzle, and W. C. Hamilton, Int. J. Peptide Protein Res.,4, 229 (1972).CrossRefGoogle Scholar
  12. 12.
    J. Donohue and A. Caron, Acta Cryst.,17, 1178 (1964).CrossRefGoogle Scholar
  13. 13.
    E. M. Popov, V. G. Dashevskii, G. M. Lipkind, and S. F. Arkhipova, Molekul. Biol.,2, 612 (1968).Google Scholar
  14. 14.
    D. Poland and H. A. Scheraga, Biochem.,6, 3791 (1967).CrossRefGoogle Scholar
  15. 15.
    G. M. Lipkind, S. F. Arkhipova, and E. M. Popov, Zh. Strukt. Khim.,11, 121 (1970).Google Scholar
  16. 16.
    I. A. Shellmann, Compt. Rend. Trav. Lab. Carlsberg, Ser. Chim.,29, 223 (1955).Google Scholar
  17. 17.
    G. Pimentel and O. McClellan, The Hydrogen Bond, W. H. Freeman, San Francisco (1960).Google Scholar
  18. 18.
    R. A. Scott and H. A. Scheraga, J. Chem. Phys.,45, 2091 (1966).CrossRefGoogle Scholar
  19. 19.
    H. A. Scheraga, Adv. Phys. Org. Chem.,6, 103 (1968).Google Scholar
  20. 20.
    P. N. Lewis, F. A. Momany, and H. A. Scheraga, Israel J. Chemistry,11, 121 (1973).CrossRefGoogle Scholar
  21. 21.
    H. C. Watson, Progr. Stereochemistry,4, 299 (1969).Google Scholar
  22. 22.
    J. J. Birktoft and D. M. Blow, J. Mol. Biol.,68, 187 (1972).CrossRefGoogle Scholar
  23. 23.
    F. A. Quiocho and W. N. Lipscomb, Advan. Protein Chem.,25, 1 (1971).CrossRefGoogle Scholar
  24. 24.
    H. W. Wyckoff, D. Tsernoglou, A. W. Hanson, J. R. Kuox, B. Lee, and F. M. Richard, J. Biol. Chem.,245, 305 (1970).PubMedGoogle Scholar

Copyright information

© Plenum Publishing Corporation 1977

Authors and Affiliations

  • P. Berlin
  • M. Kreisler
  • S. F. Arkhipova
  • G. M. Lipkind
  • E. M. Popov

There are no affiliations available

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