Electromagnetic-radiation absorption by water.

Why does a microwave oven work? How does biological tissue absorb electromagnetic radiation? Astonishingly, we do not have a definite answer to these simple questions because the microscopic processes governing the absorption of electromagnetic waves by water are largely unclarified. This absorption can be quantified by dielectric loss spectra, which reveal a huge peak at a frequency of the exciting electric field of about 20 GHz and a gradual tailing off toward higher frequencies. The microscopic interpretation of such spectra is highly controversial and various superpositions of relaxation and resonance processes ascribed to single-molecule or molecule-cluster motions have been proposed for their analysis. By combining dielectric, microwave, THz, and far-infrared spectroscopy, here we provide nearly continuous temperature-dependent broadband spectra of water. Moreover, we find that corresponding spectra for aqueous solutions reveal the same features as pure water. However, in contrast to the latter, crystallization in these solutions can be avoided by supercooling. As different spectral contributions tend to disentangle at low temperatures, this enables us to deconvolute them when approaching the glass transition under cooling. We find that the overall spectral development, including the 20 GHz feature (employed for microwave heating), closely resembles the behavior known for common supercooled liquids. Thus water's absorption of electromagnetic waves at room temperature is not unusual but very similar to that of glass-forming liquids at elevated temperatures, deep in the low-viscosity liquid regime, and should be interpreted along similar lines.

Dynamics of protein hydration water.

We present the frequency- and temperature-dependent dielectric properties of lysozyme solutions in a broad concentration regime, measured at subzero temperatures, and compare the results with measurements above the freezing point of water and on hydrated lysozyme powder. Our experiments allow examining the dynamics of unfreezable hydration water in a broad temperature range. The obtained results prove the bimodality of the hydration shell dynamics. In addition, we find indications of a fragile-to-strong transition of hydration water.

Liquid 1-propanol studied by neutron scattering, near-infrared, and dielectric spectroscopy.

Liquid monohydroxy alcohols exhibit unusual dynamics related to their hydrogen bonding induced structures. The connection between structure and dynamics is studied for liquid 1-propanol using quasi-elastic neutron scattering, combining time-of-flight and neutron spin-echo techniques, with a focus on the dynamics at length scales corresponding to the main peak and the pre-peak of the structure factor. At the main peak, the structural relaxation times are probed. These correspond well to mechanical relaxation times calculated from literature data. At the pre-peak, corresponding to length scales related to H-bonded structures, the relaxation times are almost an order of magnitude longer. According to previous work [C. Gainaru, R. Meier, S. Schildmann, C. Lederle, W. Hiller, E. Rössler, and R. Böhmer, Phys. Rev. Lett. 105, 258303 (2010)] this time scale difference is connected to the average size of H-bonded clusters. The relation between the relaxation times from neutron scattering and those determined from dielectric spectroscopy is discussed on the basis of broad-band permittivity data of 1-propanol. Moreover, in 1-propanol the dielectric relaxation strength as well as the near-infrared absorbance reveal anomalous behavior below ambient temperature. A corresponding feature could not be found in the polyalcohols propylene glycol and glycerol.

Relaxation dynamics of a protein solution investigated by dielectric spectroscopy.

In the present work, we provide a dielectric study on two differently concentrated aqueous lysozyme solutions in the frequency range from 1MHz to 40GHz and for temperatures from 275 to 330K. We analyze the three dispersion regions, commonly found in protein solutions, usually termed ß-, γ-, and δ-relaxations. The ß-relaxation, occurring in the frequency range around 10MHz and the γ-relaxation around 20GHz (at room temperature) can be attributed to the rotation of the polar protein molecules in their aqueous medium and the reorientational motion of the free water molecules, respectively. The nature of the δ-relaxation, which is often ascribed to the motion of bound water molecules, is not yet fully understood. Here we provide data on the temperature dependence of the relaxation times and relaxation strengths of all three detected processes and on the dc conductivity arising from ionic charge transport. The temperature dependences of the ß- and γ-relaxations are closely correlated. We found a significant temperature dependence of the dipole moment of the protein, indicating conformational changes. Moreover we find a breakdown of the Debye-Stokes-Einstein relation in this protein solution, i.e., the dc conductivity is not completely governed by the mobility of the solvent molecules. Instead it seems that the dc conductivity is closely connected to the hydration shell dynamics.

Broadband dielectric spectroscopy on human blood.

BACKGROUND: Dielectric spectra of human blood reveal a rich variety of dynamic processes. Achieving a better characterization and understanding of these processes not only is of academic interest but also of high relevance for medical applications as, e.g., the determination of absorption rates of electromagnetic radiation by the human body. METHODS: The dielectric properties of human blood are studied using broadband dielectric spectroscopy, systematically investigating the dependence on temperature and hematocrit value. By covering a frequency range from 1Hz to 40GHz, information on all the typical dispersion regions of biological matter is obtained. RESULTS AND CONCLUSIONS: We find no evidence for a low-frequency relaxation ("α-relaxation") caused, e.g., by counterion diffusion effects as reported for some types of biological matter. The analysis of a strong Maxwell-Wagner relaxation arising from the polarization of the cell membranes in the 1-100MHz region ("ß-relaxation") allows for the test of model predictions and the determination of various intrinsic cell properties. In the microwave region beyond 1GHz, the reorientational motion of water molecules in the blood plasma leads to another relaxation feature ("γ-relaxation"). Between ß- and γ-relaxations, significant dispersion is observed, which, however, can be explained by a superposition of these relaxation processes and is not due to an additional "δ-relaxation" often found in biological matter. GENERAL SIGNIFICANCE: Our measurements provide dielectric data on human blood of so far unsurpassed precision for a broad parameter range. All data are provided in electronic form to serve as basis for the calculation of the absorption rate of electromagnetic radiation and other medical purposes. Moreover, by investigating an exceptionally broad frequency range, valuable new information on the dynamic processes in blood is obtained.

Dielectric spectroscopy on aqueous electrolytic solutions.

In this work, detailed dielectric measurements are presented on aqueous electrolytic solutions of NaCl and KCl in a broad frequency range, typical for modern telecommunication techniques. The complex dielectric permittivity or equivalently the complex conductivity are systematically studied as function of frequency (100 MHz-40 GHz), temperature (10-60 degrees C) and molar concentration (0.001-1 mol/l). By a detailed analysis of the dielectric results using an asymmetrically broadened Cole-Davidson distribution of relaxation times, in addition to dc conductivity, the dielectric response as function of frequency, temperature, and molar concentration was fully parameterized by a total of 13 parameters. This model ansatz and the 13 parameters include an enormous predictive power, allowing a reasonable estimation of the dielectric constant, loss, and the conductivity for any set of external variables frequency, temperature and concentration. The proposed method is not only useful for rather simple electrolytic solutions, but also for cell suspensions and biological matter, if additional processes, especially at low frequencies, are adequately taken into account.