Hydration-dependent dynamic crossover phenomenon in protein hydration water
Name
PhysRevE.90.042705.pdf
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1.1 MB
Format
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Checksum (MD5)
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Author(s)
Wang, Zhe
Fratini, Emiliano
Li, Mingda
Le, Peisi
Mamontov, Eugene
Baglioni, Piero
Chen, Sow-Hsin
Date Issued
October 2014
Journal
Physical Review E
Publisher
American Physical Society
Citation
Wang, Zhe, et al. "Hydration-dependent dynamic crossover phenomenon in protein hydration water." Phys. Rev. E 90, 042705 (October 2014). © 2014 American Physical Society
Version
Final published version
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 h[subscript c] =0.2–0.25 and becomes more visible as h increases. When h is lower than h[subscript c], 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.
MIT Department
Massachusetts Institute of Technology. Department of Nuclear Science and Engineering
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DOI of Published Version
https://doi.org/10.1103/PhysRevE.90.042705
