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Title: Some thermodynamical aspects of protein hydration water

Abstract

We study by means of nuclear magnetic resonance the self-diffusion of protein hydration water at different hydration levels across a large temperature range that includes the deeply supercooled regime. Starting with a single hydration shell (h = 0.3), we consider different hydrations up to h = 0.65. Our experimental evidence indicates that two phenomena play a significant role in the dynamics of protein hydration water: (i) the measured fragile-to-strong dynamic crossover temperature is unaffected by the hydration level and (ii) the first hydration shell remains liquid at all hydrations, even at the lowest temperature.

Authors:
 [1];  [1];  [2];  [1];  [3];  [4];  [5]
  1. Dipartimento di Fisica e Scienze della Terra, Università di Messina and CNISM, I-98168 Messina (Italy)
  2. Dipartimento SASTAS, Università di Messina, I-98166 Messina (Italy)
  3. CNR-IPCF, Viale F. Stagno D’Alcontres 37, I-98158 Messina (Italy)
  4. Center for Polymer Studies and Department of Physics, Boston University, Boston, Massachusetts 02215 (United States)
  5. Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 (United States)
Publication Date:
OSTI Identifier:
22415955
Resource Type:
Journal Article
Journal Name:
Journal of Chemical Physics
Additional Journal Information:
Journal Volume: 142; Journal Issue: 21; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0021-9606
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; HYDRATION; LIQUIDS; NUCLEAR MAGNETIC RESONANCE; PROTEINS; SELF-DIFFUSION; TEMPERATURE DEPENDENCE; WATER

Citation Formats

Mallamace, Francesco, Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, Center for Polymer Studies and Department of Physics, Boston University, Boston, Massachusetts 02215, Corsaro, Carmelo, CNR-IPCF, Viale F. Stagno D’Alcontres 37, I-98158 Messina, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Stanley, H. Eugene, and Chen, Sow-Hsin. Some thermodynamical aspects of protein hydration water. United States: N. p., 2015. Web. doi:10.1063/1.4921897.
Mallamace, Francesco, Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, Center for Polymer Studies and Department of Physics, Boston University, Boston, Massachusetts 02215, Corsaro, Carmelo, CNR-IPCF, Viale F. Stagno D’Alcontres 37, I-98158 Messina, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Stanley, H. Eugene, & Chen, Sow-Hsin. Some thermodynamical aspects of protein hydration water. United States. doi:10.1063/1.4921897.
Mallamace, Francesco, Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, Center for Polymer Studies and Department of Physics, Boston University, Boston, Massachusetts 02215, Corsaro, Carmelo, CNR-IPCF, Viale F. Stagno D’Alcontres 37, I-98158 Messina, Mallamace, Domenico, Vasi, Sebastiano, Vasi, Cirino, Stanley, H. Eugene, and Chen, Sow-Hsin. Sun . "Some thermodynamical aspects of protein hydration water". United States. doi:10.1063/1.4921897.
@article{osti_22415955,
title = {Some thermodynamical aspects of protein hydration water},
author = {Mallamace, Francesco and Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and Center for Polymer Studies and Department of Physics, Boston University, Boston, Massachusetts 02215 and Corsaro, Carmelo and CNR-IPCF, Viale F. Stagno D’Alcontres 37, I-98158 Messina and Mallamace, Domenico and Vasi, Sebastiano and Vasi, Cirino and Stanley, H. Eugene and Chen, Sow-Hsin},
abstractNote = {We study by means of nuclear magnetic resonance the self-diffusion of protein hydration water at different hydration levels across a large temperature range that includes the deeply supercooled regime. Starting with a single hydration shell (h = 0.3), we consider different hydrations up to h = 0.65. Our experimental evidence indicates that two phenomena play a significant role in the dynamics of protein hydration water: (i) the measured fragile-to-strong dynamic crossover temperature is unaffected by the hydration level and (ii) the first hydration shell remains liquid at all hydrations, even at the lowest temperature.},
doi = {10.1063/1.4921897},
journal = {Journal of Chemical Physics},
issn = {0021-9606},
number = 21,
volume = 142,
place = {United States},
year = {2015},
month = {6}
}