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 language | English |
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Pages (from-to) | 211-215 |
Number of pages | 5 |
Journal | Progress in Colloid and Polymer Science |
Volume | 83 |
DOIs | |
State | Published - 1990 |
Externally published | Yes |
Keywords
- Bovine serumalbumin
- Myoglobin single crystals
- NMR field gradient technique
- Percolation transitions