Publication | Closed Access
Conductivity in Hydrated Proteins: No Signs of the Fragile-to-Strong Crossover
110
Citations
24
References
2008
Year
Protein ChemistryBiochemistryHydrated ProteinsProtein FoldingMembrane TransportHydrated ProteinCusplike Solvent BehaviorNatural SciencesMolecular BiologyBiophysical AspectPhysical ChemistryProtein RefoldingMedicineBiophysicsHydration Water
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.
| Year | Citations | |
|---|---|---|
Page 1
Page 1