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. 2008 Mar 14;100(10):108103.
doi: 10.1103/PhysRevLett.100.108103. Epub 2008 Mar 14.

Conductivity in hydrated proteins: no signs of the fragile-to-strong crossover

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Conductivity in hydrated proteins: no signs of the fragile-to-strong crossover

S Pawlus et al. Phys Rev Lett. .

Abstract

Dielectric spectroscopy studies of hydrated protein demonstrate smooth temperature variations of conductivity. This observation suggests no cusplike fragile-to-strong crossover (FSC) in the protein's hydration water. The FSC at T approximately 220 K was postulated recently on the basis of neutron scattering studies [Chen, Proc. Natl. Acad. Sci. U.S.A. 103, 9012 (2006)] and was proposed to be the main cause for the dynamic transition in hydrated proteins. Following Swenson et al. , we ascribe the neutron results to a secondary relaxation. We emphasize that no cusplike solvent behavior is required for the protein's dynamic transition.

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