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NMR study of diffusion in protein hydration shells

  • Dispersed Systems
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Interfaces in Condensed Systems

Part of the book series: Progress in Colloid & Polymer Science ((PROGCOLLOID,volume 83))

Abstract

Water diffusion coefficients have been measured in myoglobin single crystals and bovine serum albumin (BSA) solutions by the aid of the NMR field-gradient technique. The temperature and the concentration dependences have been determined. The diffusion coefficients in the myoglobin single crystals and in the hydration water of the BSA solutions indicate a strikingly high mobility of the water molecules. Percolation transitions have been observed with respect to the hydration shells and the free water phase as well.

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Author information

Authors and Affiliations

  1. Institut für Molekulare Biophysik, Universität Mainz, Mainz, FRG

    F. Parak

  2. Sektion Kernresonanzspektroskopie, Universität Ulm, 7900, Ulm, FRG

    K. Kotitschke, R. Kimmich, E. Rommel & F. Parak

Authors
  1. K. Kotitschke
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  2. R. Kimmich
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  3. E. Rommel
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  4. F. Parak
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Editor information

G. H. Findenegg

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© 1990 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG

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Kotitschke, K., Kimmich, R., Rommel, E., Parak, F. (1990). NMR study of diffusion in protein hydration shells. In: Findenegg, G.H. (eds) Interfaces in Condensed Systems. Progress in Colloid & Polymer Science, vol 83. Steinkopff. https://doi.org/10.1007/BFb0116262

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  • DOI: https://doi.org/10.1007/BFb0116262

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  • Publisher Name: Steinkopff

  • Print ISBN: 978-3-7985-0840-8

  • Online ISBN: 978-3-7985-1686-1

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