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摘要
A dielectric relaxation study of aqueous solutions of the amphiphilic model peptide N-acetyl-leucine amide (NALA) at 298 K over a wide range of hydration levels is presented. The experiments range from states where water builds up several hydration layers to states where single water molecules or small water clusters are shared by several NALA molecules. The dielectric spectra reveal two modes on the 70 and 100ps timescales. These are largely broadened with regard to the Lorentzian shape caused by simple Debye-type relaxation, and are well described by the Kohlrausch-Williams-Watts stretched exponential function. The fast mode is assigned to water reorientation comprising bulk water as well as hydration water. Even when all water molecules are in contact with the solute, this fast component is dominant, and its mean relaxation time is retarded by less than a factor of two relative to neat water. The amplitude of the slow process is far higher than expected for the dipolar reorientation of the solute. The observations are consistent with results from molecular dynamics simulations for a similar model peptide reported in the literature. They suggest that the slow relaxation mode is mainly founded in petide-water dipolar couplings, with some additional contribution from slowly reorienting hydration water molecules. The results are discussed with regard to the hydration dynamics, of proteins and the interpretation of dielectric spectra of protein solutions.
- 出版日期2008-12-22
