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000011792 0247_ $$2DOI$$a10.1103/PhysRevLett.104.098101
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000011792 084__ $$2WoS$$aPhysics, Multidisciplinary
000011792 1001_ $$0P:(DE-HGF)0$$aDoster, W.$$b0
000011792 245__ $$aDynamical Transition of Protein-Hydration Water
000011792 260__ $$aCollege Park, Md.$$bAPS$$c2010
000011792 300__ $$a098101
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000011792 440_0 $$04925$$aPhysical Review Letters$$v104$$x0031-9007$$y9
000011792 500__ $$aThis work has been supported by Deutsche Forschungsgemeinschaft through SFB 533. We thank the late Henry Crespi for providing D-CPC.
000011792 520__ $$aThin layers of water on biomolecular and other nanostructured surfaces can be supercooled to temperatures not accessible with bulk water. Chen et al. [Proc. Natl. Acad. Sci. U.S.A. 103, 9012 (2006)] suggested that anomalies near 220 K observed by quasielastic neutron scattering can be explained by a hidden critical point of bulk water. Based on more sensitive measurements of water on perdeuterated phycocyanin, using the new neutron backscattering spectrometer SPHERES, and an improved data analysis, we present results that show no sign of such a fragile-to-strong transition. The inflection of the elastic intensity at 220 K has a dynamic origin that is compatible with a calorimetric glass transition at 170 K. The temperature dependence of the relaxation times is highly sensitive to data evaluation; it can be brought into perfect agreement with the results of other techniques, without any anomaly.
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000011792 7001_ $$0P:(DE-HGF)0$$aBusch, S.$$b1
000011792 7001_ $$0P:(DE-HGF)0$$aGaspar, A.M.$$b2
000011792 7001_ $$0P:(DE-Juel1)VDB95094$$aAppavou, M.-S.$$b3$$uFZJ
000011792 7001_ $$0P:(DE-Juel1)131044$$aWuttke, J.$$b4$$uFZJ
000011792 7001_ $$0P:(DE-HGF)0$$aScheer, H.$$b5
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000011792 8567_ $$uhttp://dx.doi.org/10.1103/PhysRevLett.104.098101
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