TY  - JOUR
AU  - Doster, W.
AU  - Busch, S.
AU  - Gaspar, A.M.
AU  - Appavou, M.-S.
AU  - Wuttke, J.
AU  - Scheer, H.
TI  - Dynamical Transition of Protein-Hydration Water
JO  - Physical review letters
VL  - 104
SN  - 0031-9007
CY  - College Park, Md.
PB  - APS
M1  - PreJuSER-11792
SP  - 098101
PY  - 2010
N1  - This work has been supported by Deutsche Forschungsgemeinschaft through SFB 533. We thank the late Henry Crespi for providing D-CPC.
AB  - 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.
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000275252500043
DO  - DOI:10.1103/PhysRevLett.104.098101
UR  - https://juser.fz-juelich.de/record/11792
ER  -