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Title: Hydration-dependent dynamic crossover phenomenon in protein hydration water

Abstract

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.

Authors:
 [1];  [2];  [1];  [1];  [3];  [2];  [1]
+ Show Author Affiliations
  1. Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
  2. University of Florence, Sesto Fiorentino (Italy)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1505761
Alternate Identifier(s):
OSTI ID: 1180967
Grant/Contract Number:  
FG02-90ER45429
Resource Type:
Accepted Manuscript
Journal Name:
Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
Additional Journal Information:
Journal Volume: 90; Journal Issue: 4; Journal ID: ISSN 1539-3755
Publisher:
American Physical Society (APS)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Wang, Zhe, Fratini, Emiliano, Li, Mingda, Le, Peisi, Mamontov, Eugene, Baglioni, Piero, and Chen, Sow-Hsin. Hydration-dependent dynamic crossover phenomenon in protein hydration water. United States: N. p., 2014. Web. doi:10.1103/physreve.90.042705.
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Wang, Zhe, Fratini, Emiliano, Li, Mingda, Le, Peisi, Mamontov, Eugene, Baglioni, Piero, & Chen, Sow-Hsin. Hydration-dependent dynamic crossover phenomenon in protein hydration water. United States. https://doi.org/10.1103/physreve.90.042705
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Wang, Zhe, Fratini, Emiliano, Li, Mingda, Le, Peisi, Mamontov, Eugene, Baglioni, Piero, and Chen, Sow-Hsin. Wed . "Hydration-dependent dynamic crossover phenomenon in protein hydration water". United States. https://doi.org/10.1103/physreve.90.042705. https://www.osti.gov/servlets/purl/1505761.
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@article{osti_1505761,
title = {Hydration-dependent dynamic crossover phenomenon in protein hydration water},
author = {Wang, Zhe and Fratini, Emiliano and Li, Mingda and Le, Peisi and Mamontov, Eugene and Baglioni, Piero and Chen, Sow-Hsin},
abstractNote = {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.},
doi = {10.1103/physreve.90.042705},
journal = {Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics},
number = 4,
volume = 90,
place = {United States},
year = {Wed Oct 08 00:00:00 EDT 2014},
month = {Wed Oct 08 00:00:00 EDT 2014}
}
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Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1103/physreve.90.042705
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Citation Metrics:
Cited by: 11 works
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Figures / Tables:

FIG. 1 FIG. 1: Quasielastic neutron scattering spectra of the hydration water at (a) T = 295 K and (b) 235 K for the sample with h = 0.30 (red open squares) and 0.45 (green open circles) at Q = 0.5 Å−1. The fitted curves are denoted by solid lines. At 295more » K, the protein hydration water at h = 0.30 is seen to relax more slowly than the one at h = 0.45. However, this ordering is reversed at 235 K.« less
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    Works referencing / citing this record:

    Some thermodynamical aspects of protein hydration water
    journal, June 2015

    • Mallamace, Francesco; Corsaro, Carmelo; Mallamace, Domenico
    • The Journal of Chemical Physics, Vol. 142, Issue 21
    • DOI: 10.1063/1.4921897
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      Figures / Tables found in this record:

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      TABLE I (p. 4)table
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