Journal Article PreJuSER-11792

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Dynamical Transition of Protein-Hydration Water

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2010
APS College Park, Md.

Physical review letters 104, 098101 () [10.1103/PhysRevLett.104.098101]

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Abstract: Thin layers of water on biomolecular and other nanostructured surfaces can be supercooled to temperatures not accessible with bulk water. Chen et al. [Proc. Natl. Acad. Sci. U.S.A. 103, 9012 (2006)] suggested that anomalies near 220 K observed by quasielastic neutron scattering can be explained by a hidden critical point of bulk water. Based on more sensitive measurements of water on perdeuterated phycocyanin, using the new neutron backscattering spectrometer SPHERES, and an improved data analysis, we present results that show no sign of such a fragile-to-strong transition. The inflection of the elastic intensity at 220 K has a dynamic origin that is compatible with a calorimetric glass transition at 170 K. The temperature dependence of the relaxation times is highly sensitive to data evaluation; it can be brought into perfect agreement with the results of other techniques, without any anomaly.

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Note: This work has been supported by Deutsche Forschungsgemeinschaft through SFB 533. We thank the late Henry Crespi for providing D-CPC.

Contributing Institute(s):
  1. Streumethoden (IFF-4)
  2. Neutronenstreuung (IFF-5)
  3. JCNS (Jülich Centre for Neutron Science JCNS (JCNS) ; JCNS)
Research Program(s):
  1. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)
  2. Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI) (P55)
Experiment(s):
  1. SPHERES: Backscattering spectrometer (NL6S)

Appears in the scientific report 2010
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