Published June 7, 2015 | Version v1
Journal article

Some thermodynamical aspects of protein hydration water

  • 1. Center for Polymer Studies and Department of Physics, Boston University, Boston, Massachusetts 02215 (United States)
  • 2. Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 (United States)
  • 3. Dipartimento di Fisica e Scienze della Terra, Università di Messina and CNISM, I-98168 Messina (Italy)
  • 4. CNR-IPCF, Viale F. Stagno D'Alcontres 37, I-98158 Messina (Italy)
  • 5. Dipartimento SASTAS, Università di Messina, I-98166 Messina (Italy)

Description

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

Additional details

Identifiers

Publishing Information

Journal Title
Journal of Chemical Physics
Journal Volume
142
Journal Issue
21
Journal Page Range
p. 215103-215103.5
ISSN
0021-9606
CODEN
JCPSA6

INIS

Country of Publication
United States
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46121847
Subject category
S37: INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY;
Descriptors DEI
HYDRATION; LIQUIDS; NUCLEAR MAGNETIC RESONANCE; PROTEINS; SELF-DIFFUSION; TEMPERATURE DEPENDENCE; WATER
Descriptors DEC
DIFFUSION; FLUIDS; HYDROGEN COMPOUNDS; MAGNETIC RESONANCE; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; RESONANCE; SOLVATION

Optional Information

Notes
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