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