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 |
|---|---|
| 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