Hydration-dependent dynamic crossover phenomenon in protein hydration water
Journal Article
·
· Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
- Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
- University of Florence, Sesto Fiorentino (Italy)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
We present 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. Furthermore, 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.
- Research Organization:
- Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- FG02-90ER45429
- OSTI ID:
- 1505761
- Alternate ID(s):
- OSTI ID: 1180967
- Journal Information:
- Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics, Vol. 90, Issue 4; ISSN 1539-3755
- Publisher:
- American Physical Society (APS)Copyright Statement
- Country of Publication:
- United States
- Language:
- English
Cited by: 11 works
Citation information provided by
Web of Science
Web of Science
Some thermodynamical aspects of protein hydration water
|
journal | June 2015 |
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