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17O NMR Studies of Solid Amino Acids

  • D. Fiat
  • J. Tritt-Goc
  • R. Goc
Conference paper

Abstract

17O nmr quadrupolar echo experiments have been performed of polycrystalline 1-leucine in order to gain better insight into its crystalline structure and dynamics of molecular motion primarily of the structural aspects of N – HO hydrogen bonds. The central transition (m-1/2 < — > -1/2) NMR spectrum was derived by Fourier transforming the second half of the quadrupolar echo signal. The spectrum was further analyzed by a numerical method. L-leucine was enriched to about 20% in 17 O and studies were carried out in a magnetic field of 4.23 T (17O Larmor frequency 24.4 MHz). The measurements were performed in the temperature range of -50°C to 80°C. The room temperature (26°C) spectrum consists of two lines, each having a shape typical to NMR powder pattern of a central transition in the case when second order quadrupolar perturbation is significant.

PACS number

76.60 

References

  1. 1.
    M. M. Harding, and R. M. Howieson.. Acta Crvst. B32. 633 (1976)CrossRefGoogle Scholar
  2. 2.
    M. Coll, Acta Cryst., C42, 599 (1986).Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1990

Authors and Affiliations

  • D. Fiat
    • 1
  • J. Tritt-Goc
    • 1
    • 2
  • R. Goc
    • 1
  1. 1.Department of Physiology and BiophysicsUniversity of Illinois at ChicagoChicagoUSA
  2. 2.Institute of Molecular PhysicsPoznanPoland

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