Subnanosecond Time Range Research Articles

Investigation of the switching characteristics of high-pressure subnanosecond gas dischargers with the purpose of a sharp increasing of the breakdown voltages and the switching speed

The paper analyzes the data obtained in the subnanosecond time range on the times (t br) and speeds (V br) of switching of hydrogen diode dischargers. These data were obtained in a wide range of hydrogen pressures (p) and the degree of the discharge gap overvoltage (the length of the cathode–anode gap d) in a uniform electric field. It is shown that the reduced strength of the average electric field E br/p in the discharge gap at the moment of the beginning of the breakdown significantly decreases when the gas pressure increases from 5 atm to 50 atm. An increase in pressure from 50 atm to 60 atm leads to a sharp (by 40% ÷ 135%, depending on the d) increase in the pulse breakdown voltage (U br) and an increase in E br/p. In proportion to the growth of E br/p the switching speed V br of the discharge gas gap increases. The observed effect is explained by the change in the discharge initiation mechanisms. The limitation of U br and V br in the hydrogen pressure range from 5 atm to 50 atm occurs as a result of gas ionization by runaway electrons and the subsequent development of a multi-avalanche discharge in the volume of the discharge gap. With a further increase in pressure, the discharge develops according to the streamer type. To design ultrafast gas dischargers of the subnanosecond range intended for switching high voltages, it is necessary to select an appropriate range of working gas pressures in order to ensure the development of a streamer-type discharge.

Phosphate Vibrations Probe Electric Fields in Hydrated Biomolecules: Spectroscopy, Dynamics, and Interactions.

Electric interactions have a strong impact on the structure and dynamics of biomolecules in their native water environment. Given the variety of water arrangements in hydration shells and the femto- to subnanosecond time range of structural fluctuations, there is a strong quest for sensitive noninvasive probes of local electric fields. The stretching vibrations of phosphate groups, in particular the asymmetric (PO2)− stretching vibration νAS(PO2)−, allow for a quantitative mapping of dynamic electric fields in aqueous environments via a field-induced redshift of their transition frequencies and concomitant changes of vibrational line shapes. We present a systematic study of νAS(PO2)− excitations in molecular systems of increasing complexity, including dimethyl phosphate (DMP), short DNA and RNA duplex structures, and transfer RNA (tRNA) in water. A combination of linear infrared absorption, two-dimensional infrared (2D-IR) spectroscopy, and molecular dynamics (MD) simulations gives quantitative insight in electric-field tuning rates of vibrational frequencies, electric field and fluctuation amplitudes, and molecular interaction geometries. Beyond neat water environments, the formation of contact ion pairs of phosphate groups with Mg2+ ions is demonstrated via frequency upshifts of the νAS(PO2)− vibration, resulting in a distinct vibrational band. The frequency positions of contact geometries are determined by an interplay of attractive electric and repulsive exchange interactions.

The mutual interactions of RNA, counterions and water - quantifying the electrostatics at the phosphate-water interface.

The structure and dynamics of polyanionic biomolecules, like RNA, are decisively determined by their electric interactions with the water molecules and the counterions in the environment. The solvation dynamics of the biomolecules involves a subtle balance of non-covalent and many-body interactions with structural fluctuations due to thermal motion occurring in a femto- to subnanosecond time range. This complex fluctuating many particle scenario is crucial in defining the properties of biological interfaces with far reaching significance for the folding of RNA structures and for facilitating RNA–protein interactions. Given the inherent complexity, suited model systems, carefully calibrated and benchmarked by experiments, are required to quantify the relevant interactions of RNA with the aqueous environment. In this feature article we summarize our recent progress in the understanding of the electrostatics at the biological interface of double stranded RNA (dsRNA) and transfer RNA (tRNA). Dimethyl phosphate (DMP) is introduced as a viable and rigorously accessible model system allowing the interaction strength with water molecules and counterions, their relevant fluctuation timescales and the spatial reach of interactions to be established. We find strong (up to ≈90 MV cm−1) interfacial electric fields with fluctuations extending up to ≈20 THz and demonstrate how the asymmetric stretching vibration νAS(PO2)− of the polarizable phosphate group can serve as the most sensitive probe for interfacial interactions, establishing a rigorous link between simulations and experiment. The approach allows for the direct interfacial observation of interactions of biologically relevant Mg2+ counterions with phosphate groups in contact pair geometries via the rise of a new absorption band imposed by exchange repulsion interactions at short interatomic distances. The systematic extension to RNA provides microscopic insights into the changes of the hydration structure that accompany the temperature induced melting of the dsRNA double helix and quantify the ionic interactions in the folded tRNA. The results show that pairs of negatively charged phosphate groups and Mg2+ ions represent a key structural feature of RNA embedded in water. They highlight the importance of binding motifs made of contact pairs in the electrostatic stabilization of RNA structures that have a strong impact on the surface potential and enable the fine tuning of the local electrostatic properties which are expected to be relevant for mediating the interactions between biomolecules.

Ultrafast Radiative Relaxation Processes in Multication Cross-Luminescence Materials

Scintillators with ultrafast response are of demand in medical imaging for time-of-flight positron emission tomography, in high-energy physics calorimetry, and in other applications. There are several fast luminescence processes in solid-state materials, which could be good candidates for fast timing applications. The development of new ultrafast silicon photomultipliers with increased vacuum-ultraviolet to ultraviolet (VUV-UV) sensitivity has renewed interest to one of those, cross-luminescence (CL), emitted in the VUV-UV region with subnanosecond decay time. Previous investigations have shown that CL is mostly situated in the VUV region in binary K and Ba compounds, but ternary fluorides with a complex valence band structure can provide ultrafast emissions in UV. According to the band structure calculations for K2SiF6, its complex valence band is composed of the F 2p, Si 2s, and Si 2p states. Transitions between the valence subbands and the outermost K 3p core band may extend CL from the VUV-UV to the visible region. This motivated us to perform spectroscopic study of phase-pure K2SiF6 micropowders with a high degree of crystallinity. The stationary (10 keV) and pulsed (100 keV, $\delta t \approx 55$ ps) electron beams were applied in the studies of relaxation processes of K2SiF6 in the temperature range of 77–300 K. At 300 K, the dynamics of ultrafast processes was studied at the FemtoMAX beamline (MAX IV Lab) providing 10-keV X-ray pulses of 100-fs duration. As a result, we revealed multiple CL bands extending from 9 to 4 eV. A nonexponential decay in the subnanosecond time range was revealed for the CL bands at 4.5 and 5.25 eV under both pulsed electron-beam and X-ray excitations. This opens prospects for a band structure engineering approach in developing new ultrafast scintillators with intrinsic emissions. This approach is based on a targeted modification of material composition to influence the density of states in complex valence bands and to provide a favorable shift of CL to lower energies.

Coexistence of Femtosecond- and Nonelectron-Injecting Dyes in Dye-Sensitized Solar Cells: Inhomogeniety Limits the Efficiency

We performed a detailed and quantitative spectroscopic study of the electron injection dynamics for porphyrin as one of organic dyes at an adequate level to discuss the dye-sensitized solar cell performance. The electron injection kinetics and the electron injection yield for dye-sensitized TiO2 electrodes in redox-containing electrolytes were measured by femtosecond transient absorption and picosecond fluorescence spectroscopy. By comparing the dynamics of two of the most studied porphyrins with those of a Ru complex (N719), we have directly elucidated that the short-circuit current for the porphyrin-sensitized solar cells is limited by the presence of excited dyes that are quenched in the subnanosecond time range without competing with the electron injection process, even though both porphyrins shows faster injection processes within the picosecond time range than N719. Therefore, it was clearly indicated the electron injection efficiency was mainly limited by the inhomogeniety, which should be carefull...

The effect of Glu75 of staphylococcal nuclease on enzyme activity, protein stability and protein unfolding.

Staphylococcal nuclease mutants, E57G and E75G, were generated. A comparison of the kinetic parameters both for mutants and wild-type protein shows that the Michaelis constants (Km) were almost identical for the wild-type protein and E57G mutant. An approximately 30-fold decrease in Km compared with the wild-type protein was observed for the E75G mutant. The turnover numbers for the enzyme (kcat) were higher with both the wild-type protein and the E57G mutant (3.88 +/- 0.21 x 103 s-1 and 3.71 +/- 0.28 x 103 s-1) than with the E75G mutant (3.04 +/- 0.02 x 102 s-1). The results of thermal denaturation with differential scanning microcalorimetry indicate that the excess calorimetric enthalpy of denaturations, DeltaHcal, was almost identical for the wild-type protein and E57G mutant (84.1 +/- 6.2 kcal.mol-1 and 79.3 +/- 7.1 kcal.mol-1, respectively). An approximately twofold decrease in DeltaHcal compared with the wild-type protein was observed for the E75G mutant (42.7 +/- 5.5 kcal.mol-1). These outcomes imply that Glu at position 75 plays a significant role in maintaining enzyme activity and protein stability. Further study of the unfolding of the wild-type protein and E75G mutant was conducted by using time-resolved fluorescence with a picosecond laser pulse. Two fluorescent lifetimes were found in the subnanosecond time range. The faster lifetime (tau2) did not generally vary with either pH or the concentration of guanidinium hydrochloride (GdmHCl) in the wild-type protein and the E75G mutant. The slow lifetime (tau1), however, did vary with these parameters and was faster as the protein is unfolded by either pH or GdmHCl denaturation. The midpoints of the transition for tau1 are pH 3.5 and 5.8 for the wild-type protein and E75G mutant, respectively, and the GdmHCl concentrations are 1.1 m and 0.6 m for the wild-type protein and E75G mutant, respectively. Parallel steady-state fluorescence measurements have also been carried out and the results are in general agreement with the time-resolved fluorescence experiments, indicating that Glu at position 75 plays an important role in protein unfolding.

Fragmentation lifetimes and the internal energy of sputtered clusters

We have compared the distribution of internal energies and fragmentation rate constants determined experimentally for sputtered Fe n + cluster ions with theoretical Molecular Dynamics computer simulations. It is found that the experimental data and the simulation are complementary with respect to the fragmentation time scale involved. While the experiment is sensitive to fragmentation times of nanoseconds and above, the simulation can provide information about the time interval ranging from femtoseconds to about one nanosecond. From the experimental data, it is found that the distribution of fragmentation rates as a function of time after the emission of the clusters follows a power law rather than an exponential decay, thus indicating a broad distribution of fragmentation rate constants. From the simulation, we conclude that this dependence continues down into the sub-nanosecond time range with, however, increasing exponent as the times get shorter. Around fragmentation times at or below 10 −12 s, the rate distribution levels off due to a maximum possible rate constant of the order of the vibrational frequency of the cluster. The fragmentation rate constants are connected with the internal energy distribution of the sputtered clusters by means of statistical RRK theory. While the average internal energy determined by experiment and simulation agree quite well, significant differences are found in the width of the respective distributions, the origin of which is attributed to the different times scales explored by both techniques.

Organic solvents identify specific ligand binding sites on protein surfaces.

Enzymes frequently recognize substrates and pharmaceutical drugs through specific binding interactions in deep pockets on the protein surface. We show how the specificity-determining substrate binding site of hen egg-white lysozyme (HEWL) can be readily identified in aqueous solution by nuclear magnetic resonance spectroscopy using small organic solvent molecules as detection probes. Exchange of magnetization between the 1H nuclei of the protein and the ligands through dipole-dipole interactions is observed which allows the modeling of their position and orientation at the binding site. Combined with site-specific binding constants measured by titration experiments with different organic solvents, the method can provide important information for rational drug design. In addition, the lifetime of nonspecific interactions of HEWL with organic solvents is shown to be in the sub-nanosecond time range.

The peculiarities of colour centre production in doped alkali halides

AbstractThe peculiarities of colour centre production and recombination in KBr, KI crystals doped with Tl, In are examined. The photostimulated dopant ion luminescence (PSL response) follows that of the F‐centre production in the subnanosecond time range. It is concluded that the radiation defects in a doped crystal are spatially distributed in the near vicinity of the dopants. To a limited extent the photo‐ and thermostimulated defect recombination also takes place near the dopant.

Hydration and protein dynamics: frequency domain fluorescence spectroscopy of proteins in reverse micelles

Lysozyme, human serum albumin (HSA), and liver alcohol dehydrogenase (LADH) have been studied in reverse micelles by frequency domain fluorescence spectroscopy. The emission of the tryptophanyl residues of the proteins was monitored. Fluorescence and anisotropy decays were measured from 2 to 350 MHz for each protein in reverse micelles and in aqueous solutions. The wide range of modulation frequencies available allowed direct monitoring of the internal motions of tryptophan residues, occurring in the subnanosecond time range, together with the whole protein rotational dynamics in the micelles. The results indicate that the rotational correlation times for the internal motions and the overall protein rotation in reverse micelles decrease with increasing water concentration. Lysozymes showed peculiar rotational dynamics which reflect denaturation occurring as the protein increases its water content in the reverse micelle. This effect was not observed for the other proteins. Dynamic measurements appear useful in understanding structural changes arising from the interactions between proteins and micellar systems. © 1991 American Chemical Society.

Picosecond optical studies of electron and hole thermalization in the band tails of a-Si:H

Using picoseconnd photomodulation we have studied band tail thermalization of photo carriers by following their trapping into defect states in doped and undoped a-Si:H. We found that electron trapping in the subnanosecond time range in doped a-Si:H is about 50 times faster than hole trapping regardless of the trap center energy.

Electroluminescence delays of light-emitting diodes in the subnanosecond time range

Electroluminescence delays of light-emitting diodes in the subnanosecond time range

Subnanosecond motions of tryptophan residues in proteins

The dynamics of protein molecules in the subnanosecond and nanosecond time range were investigated by time-resolved fluorescence polarization spectroscopy. Synchrotron radiation from a storage ring was used as a pulsed light source to excite the single tryptophan residue in a series of proteins. The full width at half maximum of the detected light pulse was 0.65 nsec, making it feasible to measure emission anisotropy kinetics in the subnanosecond time range and thereby to resolve internal rotational motions. The proteins investigated exhibit different degrees of rotational freedom of their tryptophan residue, ranging from almost no mobility to nearly complete freedom in the subnanosecond time range. The tryptophan residue of Staphylococcus aureus nuclease B (20,000 daltons) has a single rotational correlation time (varphi) of 9.9 nsec at 20 degrees C, corresponding to a rotation of the whole protein molecule. By contrast, bovine basic A1 myelin protein (18,000 daltons) exhibits varphi of 0.09 and 1.26 nsec, showing that the tryptophan residue in this protein is highly flexible. The single tryptophan of human serum albumin (69,000 daltons) has almost no rotational freedom at 8 degrees C (varphi = 31.4 nsec), whereas at 43 degrees C it rotates rapidly (varphi(1) = 0.14 nsec) within a cone of semiangle 26 degrees in addition to rotating together with the whole protein (varphi(2) = 14 nsec). Of particular interest in the large angular range (semiangle, 34 degrees ) and fast rate (varphi(1) = 0.51 nsec) of the rotational motion of the tryptophan residue in Pseudomonas aeruginosa azurin (14,000 daltons). This residue is known to be located in the hydrophobic interior of the protein. The observed amplitudes and rates of these internal motions of tryptophan residues suggest that elementary steps in functionally significant conformational changes may take place in the subnanosecond time range.