Dynamical Transition of Protein-Hydration Water

被引：163

作者：

Doster, W. ^{[1
,2
]}

Busch, S. ^{[1
,2
]}

Gaspar, A. M. ^{[1
,2
]}

Appavou, M. -S. ^{[3
]}

Wuttke, J. ^{[3
]}

Scheer, H. ^{[4
]}

机构：

[1] Tech Univ Munich, Physik Dept E 13, D-85747 Garching, Germany

[2] Tech Univ Munich, ZWE FRM 2, D-85747 Garching, Germany

[3] Forschungszentrum Julich, FRM 2, JCNS, D-85747 Garching, Germany

[4] Univ Munich, Bot Inst 2, D-80638 Munich, Germany

来源：

PHYSICAL REVIEW LETTERS | 2010年 / 104卷 / 09期

关键词：

BACKSCATTERING NEUTRON SPECTROSCOPY; MOLECULAR-DYNAMICS; THERMAL-EXPANSION; MYOGLOBIN; BEHAVIOR; TEMPERATURES; SCATTERING; CROSSOVER;

D O I：

10.1103/PhysRevLett.104.098101

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

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.

引用

页数：4

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