Dynamical Transition of Protein-Hydration Water

W. Doster, S. Busch, A. M. Gaspar, M.-S. Appavou, J. Wuttke, and H. Scheer
Phys. Rev. Lett. 104, 098101 – Published 2 March 2010

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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  • Received 22 July 2009

DOI:https://doi.org/10.1103/PhysRevLett.104.098101

©2010 American Physical Society

Authors & Affiliations

W. Doster*, S. Busch, and A. M. Gaspar

  • Physik Department E 13 and ZWE FRM II, Technische Universität München, 85747 Garching, Germany

M.-S. Appavou and J. Wuttke

  • Forschungszentrum Jülich, JCNS at FRM II, Lichtenbergstrasse 1, 85747 Garching, Germany

H. Scheer

  • Botanisches Institut II, Ludwig-Maximilians-Universität München, Menzinger Strasse 67, 80638 München, Germany

  • *wdoster@ph.tum.de

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Issue

Vol. 104, Iss. 9 — 5 March 2010

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