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Electron Paramagnetic Resonance in Single Crystals of Cupric Insulin

Nature volume 203, pages 752–754 (1964)Cite this article

Abstract

THE binding of divalent metal ions to insulin has been the subject of several investigations, both chemical and physical in nature1–6. In describing here the application of electron paramagnetic resonance (EPR) spectroscopy to this problem, we wish to emphasize the richness of the data obtainable from orientation investigations of single crystals. This information is of the following kinds: (1) the number of distinct magnetic centres; (2) the orientation with respect to the crystal axes of the symmetry axes of the magnetic centres; (3) the symmetries of the protein environments of the magnetic centres, and the ground-states of the transition metal ions; (4) the delocalization of the electrons in metal ion–protein bonds; (5) identification of protein atoms bound to metal ions when the former have nuclear magnetic moments; (6) an estimate of the distance between metal ions.

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Authors and Affiliations

  1. Department of Molecular Biology and Biophysics, Yale University, New Haven, Conn.

    ARTHUR S. BRILL & JOHN H. VENABLE JUN.

Authors
  1. ARTHUR S. BRILL
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  2. JOHN H. VENABLE JUN.
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BRILL, A., VENABLE, J. Electron Paramagnetic Resonance in Single Crystals of Cupric Insulin. Nature 203, 752–754 (1964). https://doi.org/10.1038/203752a0

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