In the present work, we provide broadband dielectric spectra showing strong electrode polarization effects for various materials, belonging to very different material classes. This includes both ionic and electronic conductors as, e.g., salt solutions, ionic liquids, human blood, and colossal-dielectricconstant materials. These data are intended to provide a broad data base enabling a critical test of the validity of phenomenological and microscopic models for electrode polarization. In the present work, the results are analyzed using a simple phenomenological equivalent-circuit description, involving a distributed parallel RC circuit element for the modeling of the weakly conducting regions close to the electrodes. Excellent fits of the experimental data are achieved in this way, demonstrating the universal applicability of this approach. In the investigated ionically conducting materials, we find the universal appearance of a second dispersion region due to electrode polarization, which is only revealed if measuring down to sufficiently low frequencies. This indicates the presence of a second charge-transport process in ionic conductors with blocking electrodes.

In the present work, we provide a dielectric study on two differently concentrated aqueous lysozyme solutions in the frequency range from 1 MHz to 40 GHz and for temperatures from 275 to 330 K. We analyze the three dispersion regions, commonly found in protein solutions, usually termed β-, γ-, and δ-relaxation. The β-relaxation, occurring in the frequency range around 10 MHz and the γ-relaxation around 20 GHz (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 often is 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 β-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.

BackgroundDielectric 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. MethodsThe 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 1 Hz to 40 GHz, information on all the typical dispersion regions of biological matter is obtained. Results and conclusionsWe 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 1-100 MHz region ("β-relaxation") allows for the test of model predictions and the determination of various intrinsic cell properties. In the microwave region beyond 1 GHz, the reorientational motion of water molecules in the blood plasma leads to another relaxation feature ("γ-relaxation"). Between β-and γ-relaxation, 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 significanceOur 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.

Molecular recognition plays a central role in many biological processes. For enzymatic reactions and slow protein-protein recognition events, turn-over rates and on-rates in the millisecond-to-second time scale have been connected to internal protein dynamics detected with atomic resolution by NMR spectroscopy, and in particular conformational sampling could be established as a mechanism for enzyme-substrate and protein-protein recognition. [1][2][3][4][5] Recent theoretical studies indicate that faster rates of conformational interconversion in the microsecond time scale might limit on-rates for protein-protein recognition. [6,7] However experimental proofs were lacking so far, mainly because such rates could not be determined accurately enough and kinetic experiments in the microsecond time range are difficult to perform.Nevertheless, for proteins and TAR-RNA, [8][9][10] recent studies based on residual dipolar couplings (RDCs) and other NMR spectroscopy techniques [11,12] have detected substantial internal dynamics in a time window from the rotational correlation time t c (one-digit nanoseconds) to approximately 50 ms, [8,[13][14][15] called the supra-t c window in the following. However, the exact rates of internal dynamics within this four orders of magnitude wide time window could not be determined.Supra-t c dynamics in ubiquitin [9] and TAR-RNA [16] could be connected to the conformational sampling required for molecular recognition. While the amplitudes of motions have been indirectly detected by RDCs and characterized in great detail, it has so far been impossible to directly observe these motions and to determine the exact rate of these supra-t c motions. In contrast, conformational sampling in enzymes occurs on a time scale that is 100 to 1000 times slower than supra-t c dynamics and therefore NMR relaxation dispersion (RD) techniques have been able to establish the functional link to enzyme kinetics with atomic resolution at physiological conditions.[1, 2, 5] However, for technical reasons, RD is not sensitive to motion faster than approximately 50 ms (RD window) and therefore does not access motion in the supra-t c window at room temperature.Here we determine the rate of interconversion between conformers of free ubiquitin by a combination of NMR RD experiments in super-cooled solution and dielectric relaxation spectroscopy (DR). Furthermore, we corroborate the motional amplitudes in the RDC-derived ensembles quantitatively with the observed amplitudes of RD and DR. The methods utilized herein can be used to directly study protein dynamics in a time range that was previously inaccessible.Significant motional amplitude in the supra-t c window has been observed using RDC measurements, and was connected to the conformational sampling for a protein in the ground

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.