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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 h c = 0.2 –0.25 and becomes more visible as h increases. When h is lower than h 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. 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]
  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:
Journal Article: 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.
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. doi:10.1103/physreve.90.042705.
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. doi:10.1103/physreve.90.042705. https://www.osti.gov/servlets/purl/1505761.
@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},
issn = {1539-3755},
number = 4,
volume = 90,
place = {United States},
year = {2014},
month = {10}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 7 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 referenced in this record:

Glass Transition and Relaxation Processes in Supercooled Water
journal, December 2004


The “Protein Dynamical Transition” Does Not Require the Protein Polypeptide Chain
journal, August 2011

  • Schirò, Giorgio; Caronna, Chiara; Natali, Francesca
  • The Journal of Physical Chemistry Letters, Vol. 2, Issue 18
  • DOI: 10.1021/jz200797g

Conductivity in Hydrated Proteins: No Signs of the Fragile-to-Strong Crossover
journal, March 2008


Puzzle of Protein Dynamical Transition
journal, June 2011

  • Magazù, Salvatore; Migliardo, Federica; Benedetto, Antonio
  • The Journal of Physical Chemistry B, Vol. 115, Issue 24
  • DOI: 10.1021/jp111421m

Inelastic X-ray Scattering Studies of the Short-Time Collective Vibrational Motions in Hydrated Lysozyme Powders and Their Possible Relation to Enzymatic Function
journal, January 2013

  • Wang, Zhe; Bertrand, Christopher E.; Chiang, Wei-Shan
  • The Journal of Physical Chemistry B, Vol. 117, Issue 4
  • DOI: 10.1021/jp312842m

Concepts and problems in protein dynamics
journal, October 2013


Suppression of the dynamic transition in surface water at low hydration levels: A study of water on rutile
journal, May 2009


Common features in the microscopic dynamics of hydration water on organic and inorganic surfaces
journal, January 2012


Effect of the Environment on the Protein Dynamical Transition: A Neutron Scattering Study
journal, August 2002


Water–protein dynamic coupling and new opportunities for probing it at low to physiological temperatures in aqueous solutions
journal, January 2012

  • Mamontov, Eugene; Chu, Xiang-qiang
  • Physical Chemistry Chemical Physics, Vol. 14, Issue 33
  • DOI: 10.1039/c2cp41443k

Observation of fragile-to-strong dynamic crossover in protein hydration water
journal, June 2006

  • Chen, S. -H.; Liu, L.; Fratini, E.
  • Proceedings of the National Academy of Sciences, Vol. 103, Issue 24
  • DOI: 10.1073/pnas.0602474103

Relaxation Processes in Supercooled Confined Water and Implications for Protein Dynamics
journal, June 2006


Fragile-to-strong liquid transition in deeply supercooled confined water
journal, January 2004

  • Faraone, A.; Liu, L.; Mou, C. -Y.
  • The Journal of Chemical Physics, Vol. 121, Issue 22
  • DOI: 10.1063/1.1832595

Collective Dynamics of Protein Hydration Water by Brillouin Neutron Spectroscopy
journal, April 2009

  • Orecchini, Andrea; Paciaroni, Alessandro; Francesco, Alessio De
  • Journal of the American Chemical Society, Vol. 131, Issue 13
  • DOI: 10.1021/ja807957p

Influence of Hydration on the Dynamics of Lysozyme
journal, October 2006


Model for single-particle dynamics in supercooled water
journal, June 1999


Proteins Remain Soft at Lower Temperatures under Pressure
journal, April 2009

  • Chu, Xiang-qiang; Faraone, Antonio; Kim, Chansoo
  • The Journal of Physical Chemistry B, Vol. 113, Issue 15
  • DOI: 10.1021/jp900557w

Dynamical Transition of Protein-Hydration Water
journal, March 2010


A unified model of protein dynamics
journal, February 2009

  • Frauenfelder, H.; Chen, G.; Berendzen, J.
  • Proceedings of the National Academy of Sciences, Vol. 106, Issue 13
  • DOI: 10.1073/pnas.0900336106

Low-frequency Vibrational Anomalies in β-Lactoglobulin:  Contribution of Different Hydrogen Classes Revealed by Inelastic Neutron Scattering
journal, December 2001

  • Orecchini, A.; Paciaroni, A.; Bizzarri, A. R.
  • The Journal of Physical Chemistry B, Vol. 105, Issue 48
  • DOI: 10.1021/jp0114889

Dynamical transition of myoglobin revealed by inelastic neutron scattering
journal, February 1989

  • Doster, Wolfgang; Cusack, Stephen; Petry, Winfried
  • Nature, Vol. 337, Issue 6209
  • DOI: 10.1038/337754a0

Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder
journal, April 1980

  • Careri, G.; Gratton, E.; Yang, P. -H.
  • Nature, Vol. 284, Issue 5756
  • DOI: 10.1038/284572a0

Bulk-solvent and hydration-shell fluctuations, similar to  - and  -fluctuations in glasses, control protein motions and functions
journal, September 2004

  • Fenimore, P. W.; Frauenfelder, H.; McMahon, B. H.
  • Proceedings of the National Academy of Sciences, Vol. 101, Issue 40
  • DOI: 10.1073/pnas.0405573101

Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides
journal, September 2012


Hydration-dependent dynamics of deeply cooled water under strong confinement
journal, April 2013


Slaving: Solvent fluctuations dominate protein dynamics and functions
journal, November 2002

  • Fenimore, P. W.; Frauenfelder, H.; McMahon, B. H.
  • Proceedings of the National Academy of Sciences, Vol. 99, Issue 25
  • DOI: 10.1073/pnas.212637899

A time-of-flight backscattering spectrometer at the Spallation Neutron Source, BASIS
journal, August 2011

  • Mamontov, E.; Herwig, K. W.
  • Review of Scientific Instruments, Vol. 82, Issue 8
  • DOI: 10.1063/1.3626214

    Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.