Journal
PHYSICAL REVIEW LETTERS
Volume 100, Issue 10, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.100.108103
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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 similar to 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. 6,9, 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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