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

S. Pawlus; S. Khodadadi; A. P. Sokolov

doi:10.1103/PhysRevLett.100.108103

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

S. Pawlus, S. Khodadadi, A. P. Sokolov

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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 220 K was postulated recently on the basis of neutron scattering studies 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.

Original language	English
Article number	108103
Journal	Physical Review Letters
Volume	100
Issue number	10
DOIs	https://doi.org/10.1103/PhysRevLett.100.108103
State	Published - Mar 14 2008
Externally published	Yes

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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 220 K was postulated recently on the basis of neutron scattering studies 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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AB - 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 220 K was postulated recently on the basis of neutron scattering studies 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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Conductivity in hydrated proteins: No signs of the fragile-to-strong crossover

Abstract

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