Abstract
The characteristic relaxation time τ of protein hydration water exhibits a strong hydration level h dependence. The dynamic crossover is observed when h is higher than the monolayer hydration level hc=0.2-0.25 and becomes more visible as h increases. When h is lower than hc, τ only exhibits Arrhenius behavior in the measured temperature range. The activation energy of the Arrhenius behavior is insensitive to h, indicating a local-like motion. Moreover, the h dependence of the crossover temperature shows that the protein dynamic transition is not directly or solely induced by the dynamic crossover in the hydration water.
| Original language | English |
|---|---|
| Article number | 042705 |
| Journal | Physical Review E - Statistical, Nonlinear, and Soft Matter Physics |
| Volume | 90 |
| Issue number | 4 |
| DOIs | |
| State | Published - Oct 8 2014 |
| Externally published | Yes |
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