NMR study of diffusion in protein hydration shells

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

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

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.

Original languageEnglish
Pages (from-to)211-215
Number of pages5
JournalProgress in Colloid and Polymer Science
Volume83
DOIs
StatePublished - 1990
Externally publishedYes

Keywords

  • Bovine serumalbumin
  • Myoglobin single crystals
  • NMR field gradient technique
  • Percolation transitions

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