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

Journal Article · · Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
 [1];  [2];  [1];  [1];  [3];  [2];  [1]
  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)

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
Citation Metrics:
Cited by: 11 works
Citation information provided by
Web of Science

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Cited By (1)

Some thermodynamical aspects of protein hydration water journal June 2015

Figures / Tables (5)