Submicrosecond Time Scale Research Articles

Nanosecond Dynamics of Photoexcited Lyotropic Liquid Crystal Structures

Home-based soft X-ray time-resolved diffraction (TR-SXD) experiments with nanosecond time resolution (10 ns) and nanometer spatial resolution were carried out at a tabletop soft X-ray plasma source (2.7-5.9 nm). The investigated system was the lyotropic liquid crystal C(16)E(7)/paraffin/glycerol/formamide/IR 5. Usually, major changes in physical, chemical, and/or optical properties of the sample result from structural changes and shrinking morphology. Here, these effects occur as a consequence of the energy absorption in the sample upon optical laser excitation in the IR regime. The variations observed are integral intensity modulations and displacement in the Bragg diffraction angle. To follow the diffracted integral intensity changes, Patterson analysis was used, and the lattice parameter d variations have been followed by applying the Bragg diffraction law. The experimental intensity modulations occur on the nanosecond time scale, and they are assigned to photoinduced diffusion processes within the liquid crystalline phase. The structural response after photoexcitation is experimentally observed as an increase of the lattice constant by 0.5-1 A and is interpreted as a decrease of order in the liquid crystalline phase. This coincides with a reorientation to a photocreated liquid crystal lattice in the surface plane and with respect to the E-field vector of the laser light. The present studies emphasize the possibility of using TR-SXD techniques for studying the transient mechanical dynamics of nanosystems at the submicrosecond time scale.

The Membrane Complex between Transducin and Dark-State Rhodopsin Exhibits Large-Amplitude Interface Dynamics on the Sub-Microsecond Timescale: Insights from All-Atom MD Simulations

Rhodopsin, the prototype class A G-protein-coupled receptor, is a very important model system for all seven-transmembrane domain proteins. Characterization of the interactions between rhodopsin and transducin, its intracellular G-protein counterpart, and the fluctuations in these interactions due to thermal motions is required for an understanding of early events in the mechanism of signal transduction. In this study, we used all-atom molecular dynamics simulations of a transmembrane protein complex between rhodopsin and the heterotrimeric transducin (Gαβγ) in an all-atom DOPC (1,2-dioleoylsn-glycero-3-phosphocholine) membrane–water environment. Based on the analysis of a microsecond-timescale simulation trajectory, we characterized the dynamics of the system and its effects in the structural features of the protein subunits. Our simulations describe a highly dynamic interaction interface where the system is alternating between distinct domain orientations at the 10- to 100-ns timescale that can be further classified into interaction modes involving contacts between distinct structural features on the protein subunits. We related our results with experimental measurements from a variety of studies and high-resolution models of activated rhodopsin. Monitoring key structural features that are involved in the activation process along our simulation trajectory indicates the presence of extensive dynamics in the dark-adapted state, including a motion of Y223 from helix 3 toward the “ionic-lock” interactions of the conserved ERY motif. The dynamic picture shown here is consistent with a framework in which the dark-state fluctuations sample conformations consistent with the activated state. These results provide an atomic-level description of the dynamics of the full complex and further suggest novel mutagenesis experiments that can be used to investigate the stability and dynamics of this model membrane protein receptor system.

Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy.

Amyloid aggregates of a C-truncated Y145Stop mutant of human prion protein, huPrP23-144, associated with a heritable amyloid angiopathy, have previously been shown to contain a compact, relatively rigid, and beta-sheet-rich approximately 30-residue amyloid core near the C-terminus under physiologically relevant conditions. In contrast, the remaining huPrP23-144 residues display considerable conformational dynamics, as evidenced by the absence of corresponding signals in cross-polarization (CP)-based solid-state NMR (SSNMR) spectra under ambient conditions and their emergence in analogous spectra recorded at low temperature on frozen fibril samples. Here, we present the direct observation of residues comprising the flexible N-terminal domain of huPrP23-144 amyloid by using 2D J-coupling-based magic-angle spinning (MAS) SSNMR techniques. Chemical shifts for these residues indicate that the N-terminal domain is effectively an ensemble of protein chains with random-coil-like conformations. Interestingly, a detailed analysis of signal intensities in CP-based 3D SSNMR spectra suggests that non-negligible molecular motions may also be occurring on the NMR time scale within the relatively rigid core of huPrP23-144 amyloid. To further investigate this hypothesis, quantitative measurements of backbone dipolar order parameters and transverse spin relaxation rates were performed for the core residues. The observed order parameters indicate that, on the submicrosecond time scale, these residues are effectively rigid and experience only highly restricted and relatively uniform motions similar to those characteristic for well-structured regions of microcrystalline proteins. On the other hand, significant variations in magnitude of transverse spin relaxation rates were noted for residues present at different locations within the core region and correlated with observed differences in spectral intensities. While interpreted only qualitatively at the present time, the extent of the observed variations in transverse relaxation rates is consistent with the presence of relatively slow, microsecond-millisecond time scale chemical exchange type phenomena within the huPrP23-144 amyloid core.

Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions

Antimicrobial peptides (AMPs) comprise a large family of peptides that include small cationic peptides, such as magainins, which permeabilize lipid membranes. Previous atomistic level simulations of magainin-H2 peptides show that they act by forming toroidal transmembrane pores. However, due to the atomistic level of description, these simulations were necessarily limited to small system sizes and sub-microsecond time scales. Here, we study the long-time relaxation properties of these pores by evolving the systems using a coarse-grain (CG) description. The disordered nature and the topology of the atomistic pores are maintained at the CG level. The peptides sample different orientations but at any given time, only a few peptides insert into the pore. Key states observed at the CG level are subsequently back-transformed to the atomistic level using a resolution-transformation protocol. The configurations sampled at the CG level are stable in the atomistic simulation. The effect of helicity on pore stability is investigated at the CG level and we find that partial helicity is required to form stable pores. We also show that the current CG scheme can be used to study spontaneous poration by magainin-H2 peptides. Overall, our simulations provide a multi-scale view of a fundamental biophysical membrane process involving a complex interplay between peptides and lipids.

An Electrohydrodynamic Model and Extensive MD Simulations Agree on the Positional and Intra-Residual Relaxations Up to Sub-Microsecond Dynamics

Our recent simulations have indicated that the number of water molecules within a cutoff distance of each residue scales linearly with protein depth. At physiological temperatures, while the translational memory of water molecules around a residue is proportional to its depth, the orientational memory is independent of the residues position[1]. These corroborate the recently reported result that water density fluctuations around hydrophobic surfaces are considerably larger than those near hydrophilic surfaces[2].We develop an efficient, simple model that characterizes protein dynamics both at picosecond and sub-microsecond timescales[3], which are coupled through conformational motions and catalysis[4]. Our approach is based on our earlier two-degree-of-freedom model, coupling the protein's fluctuations to the vicinal layer[5]. It proves to be efficient in estimating dynamic transitions in different solvents. The model emanates from geometric Brownian motion, similar in spirit to those including hydrodynamic interactions[6]. In our formulation, however, the traditional intra-molecular interactions are coupled to an electrostatic field that increases the flexibility of the regions in contact with hydrophobic residues, and almost exhibits a decoupled dynamics from hydrophilic regions where the solvent friction term dominates. We derive analytically the decay of the positional fluctuations and the relaxation of the distances between the residues which are not in direct contact.We have performed 200ns MD simulations both above and below the dynamic transitions of lysozyme and myoglobin to validate our analytical results. We obtain a remarkable agreement between simulations and our model for the decay time of both positional fluctuations and intra-residual distances.1.J.Servantie, C.Atilgan, A.R.Atilgan, ArXiv:0905-4893.2.A.J.Patel and D.Chandler, ArXiv:0909-4097.3.O.B.Okan, A.R.Atilgan, C.Atilgan, BiophysJ, Oct2009.4.W. Min, X.S. Xie, B. Bagchi, JPhysChemB, 112,454(2008).5.C. Atilgan, A.O. Aykut, A.R. Atilgan, BiophysJ, 94,79(2008).6.E. Caballero-Manrique etal, BiophysJ, 93,4128(2007).

Defect kinetics and dopant activation in submicrosecond laser thermal processes

Defect evolution in ion implanted c-Si at the submicrosecond time scales during a laser thermal annealing process is investigated by means of kinetic simulations. Nonmelting, melting, and partial melting regimes are simulated. Our modeling considers irradiation, heat diffusion, and phase transition together with defect diffusion, annihilation, and clustering. The reduction in the implantation damage and its reorganization in defect aggregates are studied as a function of the process conditions. The approach is applied to double implanted Si and compared to experimental data, indicating a relationship between damage reduction and dopant activation.

Addressing the efficiency of the energy transfer to the water flow by underwater electrical wire explosion

Experimental and hydrodynamic simulation results of submicrosecond time scale underwater electrical explosions of planar Cu and Al wire arrays are presented. A pulsed low-inductance generator having a current amplitude of up to 380 kA was used. The maximum current rise rate and maximum power achieved during wire array explosions were dI/dt≤830 A/ns and ∼10 GW, respectively. Interaction of the water flow generated during wire array explosion with the target was used to estimate the efficiency of the transfer of the energy initially stored in the generator energy to the water flow. It was shown that efficiency is in the range of 18%–24%. In addition, it was revealed that electrical explosion of the Al wire array allows almost double the energy to be transferred to the water flow due to efficient combustion of the Al wires. The latter allows one to expect a significant increase in the pressure at the front of converging strong shock waves in the case of cylindrical Al wire array underwater explosion.

Molecular Dynamics and Quantum Mechanics of RNA: Conformational and Chemical Change We Can Believe In

Structure and dynamics are both critical to RNA’s vital functions in biology. Numerous techniques can elucidate the structural dynamics of RNA, but computational approaches based on experimental data arguably hold the promise of providing the most detail. In this Account, we highlight areas wherein molecular dynamics (MD) and quantum mechanical (QM) techniques are applied to RNA, particularly in relation to complementary experimental studies.We have expanded on atomic-resolution crystal structures of RNAs in functionally relevant states by applying explicit solvent MD simulations to explore their dynamics and conformational changes on the submicrosecond time scale. MD relies on simplified atomistic, pairwise additive interaction potentials (force fields). Because of limited sampling, due to the finite accessible simulation time scale and the approximated force field, high-quality starting structures are required.Despite their imperfection, we find that currently available force fields empower MD to provide meaningful and predictive information on RNA dynamics around a crystallographically defined energy minimum. The performance of force fields can be estimated by precise QM calculations on small model systems. Such calculations agree reasonably well with the Cornell et al. AMBER force field, particularly for stacking and hydrogen-bonding interactions. A final verification of any force field is accomplished by simulations of complex nucleic acid structures.The performance of the Cornell et al. AMBER force field generally corresponds well with and augments experimental data, but one notable exception could be the capping loops of double-helical stems. In addition, the performance of pairwise additive force fields is obviously unsatisfactory for inclusion of divalent cations, because their interactions lead to major polarization and charge-transfer effects neglected by the force field. Neglect of polarization also limits, albeit to a lesser extent, the description accuracy of other contributions, such as interactions with monovalent ions, conformational flexibility of the anionic sugar−phosphate backbone, hydrogen bonding, and solute polarization by solvent. Still, despite limitations, MD simulations are a valid tool for analyzing the structural dynamics of existing experimental structures. Careful analysis of MD simulations can identify problematic aspects of an experimental RNA structure, unveil structural characteristics masked by experimental constraints, reveal functionally significant stochastic fluctuations, evaluate the structural role of base ionization, and predict structurally and potentially functionally important details of the solvent behavior, including the presence of tightly bound water molecules. Moreover, combining classical MD simulations with QM calculations in hybrid QM/MM approaches helps in the assessment of the plausibility of chemical mechanisms of catalytic RNAs (ribozymes).In contrast, the reliable prediction of structure from sequence information is beyond the applicability of MD tools. The ultimate utility of computational studies in understanding RNA function thus requires that the results are neither blindly accepted nor flatly rejected, but rather considered in the context of all available experimental data, with great care given to assessing limitations through the available starting structures, force field approximations, and sampling limitations. The examples given in this Account showcase how the judicious use of basic MD simulations has already served as a powerful tool to help evaluate the role of structural dynamics in biological function of RNA.

Molecular View of Cholesterol Flip-Flop and Chemical Potential in Different Membrane Environments

The relative stability of cholesterol in cellular membranes and the thermodynamics of fluctuations from equilibrium have important consequences for sterol trafficking and lateral domain formation. We used molecular dynamics computer simulations to investigate the partitioning of cholesterol in a systematic set of lipid bilayers. In addition to atomistic simulations, we undertook a large set of coarse grained simulations, which allowed longer time and length scales to be sampled. Our results agree with recent experiments (Steck, T. L.; et al. Biophys. J. 2002, 83, 2118-2125) that the rate of cholesterol flip-flop can be fast on physiological time scales, while extending our understanding of this process to a range of lipids. We predicted that the rate of flip-flop is strongly dependent on the composition of the bilayer. In polyunsaturated bilayers, cholesterol undergoes flip-flop on a submicrosecond time scale, while flip-flop occurs in the second range in saturated bilayers with high cholesterol content. We also calculated the free energy of cholesterol desorption, which can be equated to the excess chemical potential of cholesterol in the bilayer compared to water. The free energy of cholesterol desorption from a DPPC bilayer is 80 kJ/mol, compared to 67 kJ/mol for a DAPC bilayer. In general, cholesterol prefers more ordered and rigid bilayers and has the lowest affinity for bilayers with two polyunsaturated chains. Overall, the simulations provide a detailed molecular level thermodynamic description of cholesterol interactions with lipid bilayers, of fundamental importance to eukaryotic life.

A kinetic model of trp-cage folding from multiple biased molecular dynamics simulations.

Trp-cage is a designed 20-residue polypeptide that, in spite of its size, shares several features with larger globular proteins. Although the system has been intensively investigated experimentally and theoretically, its folding mechanism is not yet fully understood. Indeed, some experiments suggest a two-state behavior, while others point to the presence of intermediates. In this work we show that the results of a bias-exchange metadynamics simulation can be used for constructing a detailed thermodynamic and kinetic model of the system. The model, although constructed from a biased simulation, has a quality similar to those extracted from the analysis of long unbiased molecular dynamics trajectories. This is demonstrated by a careful benchmark of the approach on a smaller system, the solvated Ace-Ala3-Nme peptide. For the Trp-cage folding, the model predicts that the relaxation time of 3100 ns observed experimentally is due to the presence of a compact molten globule-like conformation. This state has an occupancy of only 3% at 300 K, but acts as a kinetic trap. Instead, non-compact structures relax to the folded state on the sub-microsecond timescale. The model also predicts the presence of a state at of 4.4 Å from the NMR structure in which the Trp strongly interacts with Pro12. This state can explain the abnormal temperature dependence of the and chemical shifts. The structures of the two most stable misfolded intermediates are in agreement with NMR experiments on the unfolded protein. Our work shows that, using biased molecular dynamics trajectories, it is possible to construct a model describing in detail the Trp-cage folding kinetics and thermodynamics in agreement with experimental data.

Investigation of Photoexcited States in Porcine Eumelanin through Their Transient Radical Products

Time-resolved electron paramagnetic resonance was used to monitor the photochemistry of radical pairs from melanin in porcine retinal pigment epithelial cells on the sub-microsecond time scale. Two distinct signals were found: one of enhanced absorption/emission at early times and one mostly emissive at later times. The emissive character of the longer lived feature suggests participation of an excited triplet precursor, something not generally thought to exist in melanins. The radicals in the early time signal were separated by about 21 A and those in the later time signal were separated by about 22-24 A.

Photo-CIDNP Study of Transient Radicals of Met-Gly and Gly-Met Peptides in Aqueous Solution at Variable pH

Time-resolved chemically induced dynamic nuclear polarization (CIDNP) was applied to the investigation of the photo-oxidation of two sulfur containing peptides, glycylmethionine (Gly-Met) and methionylglycine (Met-Gly). It was established that the reaction of Gly-Met with a photosensitizer, triplet 4-carboxybenzophenone, occurs via electron transfer from the sulfur atom and also from the terminal amino group in its uncharged state. The latter process leads to the formation of nuclear polarization of the alpha-protons of the glycine residue. The sulfur-centered cation radical of Gly-Met formed as a result of triplet quenching participates in the degenerate electron exchange reaction with the parent molecule. The rate constant of this reaction obtained from a simulation of the CIDNP kinetics is 2x10(8) M(-1) s(-1). Two channels of triplet quenching were also found for the Met-Gly peptide at pH values above the pKa of the terminal amino group: electron transfer from the amino group and from the sulfur atom. On the basis of the analysis of the CIDNP spectra and kinetics, it was found that at pH below pKa of the terminal amino group photo-oxidation of Met-Gly leads to the formation of an open-chain S-centered cation radical, which releases a proton from its N-terminal amino group to form a five-membered cyclic radical structure with a three electron bond between the S and N atoms. The rate constant of deprotonation obtained to be 1.8x10(5) s(-1) is in agreement with the pKa=4.7 of the S-centered radical of Met-Gly determined from the pH dependence of nuclear polarization. At pH>pKa, the aminium radicals formed in both peptides as a result of electron transfer from the lone pair of N-terminal amino group undergo deprotonation to the neutral aminyl radical on the submicrosecond time scale. The involvement of the different radicals was confirmed by the dependence of CIDNP on the external magnetic field ranging from 0.1 T to 7 T.

The structural basis for peptide selection by the transport receptor OppA

Oligopeptide-binding protein A (OppA) from Lactococcus lactis binds peptides of an exceptionally wide range of lengths (4-35 residues), with no apparent sequence preference. Here, we present the crystal structures of OppA in the open- and closed-liganded conformations. The structures directly explain the protein's phenomenal promiscuity. A huge cavity allows binding of very long peptides, and a lack of constraints for the position of the N and C termini of the ligand is compatible with binding of peptides with varying lengths. Unexpectedly, the peptide's amino-acid composition (but not the exact sequence) appears to have a function in selection, with a preference for proline-rich peptides containing at least one isoleucine. These properties can be related to the physiology of the organism: L. lactis is auxotrophic for branched chain amino acids and favours proline-rich caseins as a source of amino acids. We propose a new mechanism for peptide selection based on amino-acid composition rather than sequence.

Leucine-rich hydrophobic clusters promote folding of the N-terminus of the intrinsically disordered transactivation domain of p53

Molecular dynamics simulations have been performed on the intrinsically disordered 39-residue N-terminal transactivation domain of p53 (p53 1-39). Simulations not only revealed that p53 1-39 is natively compact, but also possesses a folded structure. Furthermore, leucine-rich hydrophobic clusters were found to play a crucial role in the formation and stabilization of the folded structure of p53 1-39. Collapsing in the sub-microsecond timescale might allow for rapid conformational turnovers of p53 1-39, necessary for its efficient transactivation activity and modulation. Fast collapsing might be the result of unique conformational landscapes, featuring several energy minima separated by small energy barriers. It is suggested that IDPs with highly specialized functions in the cell, such as transactivation, possibly display more ordered patterns than their less specialized counterparts.

Characterization of Different Wire Configurations in Underwater Electrical Explosion

The results of a study of shock wave (SW) generation by means of underwater electrical wire explosion with different exploding wire configurations and two high-current microsecond and submicrosecond timescale generators are presented. By using aperiodical generator discharge, a ~85% and ~15% of the stored electrical energy was transferred to the exploding wire and energy of the generated water flow, respectively. The energy of the water flow is distributed between its internal (~25%) and kinetic (~75%) energies. It was shown that the exploding wire zigzag configuration, confinement of the SW propagation region, and an increase in the rate of the energy deposition into the exploding wire allow one to increase the SW pressure ges10 times that attained with microsecond timescale straight wire explosion. The averaged thermophysical properties of nonideal and weakly degenerated plasma formed as a result of the wire explosion were obtained and summarized.

High Speed Imaging of 1 MHz Driven Microbubbles in Contact with a Rigid Wall

Since the introduction of megasonic cleaning in semiconductor industry a debate has been going on about which physical mechanism is responsible for the removal of particles. Because of the high frequency range it was believed that acoustic cavitation could not occur and cleaning was attributed to phenomena like Eckart and Schlichting streaming or pressure build-up on particles [1,2]. Recently it was shown however, that the removal of nanoparticles is closely related to the presence of acoustic cavitation in megasonic cleaning systems [3]. The dependence of particle removal efficiency on the concentration of dissolved gas and the presence of sonoluminescence are clear (but indirect) indications that the underlying mechanism is related to bubble dynamics. As the requirements for cleaning in semiconductor processing are ever more stringent, it becomes necessary to obtain a thorough understanding of the physical behavior of acoustically driven microbubbles in contact with a solid wall. In particular, the forces exerted thereby which might clean or damage a substrate are of interest. Here, a step in this direction is taken by visualization of both the removal of nanoparticles and the sub-microsecond timescale dynamics of the cavitation bubbles responsible thereof.

Non-melt laser annealing of Plasma Implanted Boron for ultra shallow junctions in Silicon

In this work we present results on sub-melt Excimer laser annealing in order to obtain difussionless activation of Boron for the creation of ultra shallow P-MOS devices. For the fulfillment of the strict requirements imposed by the ITRS roadmap for the 32 nm node we have implemented two emerging techniques: non-melt laser annealing and BF 3 Plasma Doping implantation (PLAD). By using PLAD, we were able to create ultra shallow and abrupt as implanted profiles. On the other hand, by performing laser annealing on the samples in the sub-melt regime, we can achieve high levels of electrical activation, while practically eliminating Boron diffusion, due to its capability to deliver low thermal budget in the sub-microsecond time scale. An Excimer KrF laser ( λ = 248 nm and pulse duration 38 ns) has been used. The post annealing characterization of the samples included SIMS and Van Der Pauw Sheet resistance measurements. SIMS data indicate almost difussionless dopant behavior with R s values at 680 Ω/sq. We have concluded our analysis with the examination of the morphological characteristics both of the surface of the sample using Atomic Force Microscopy (AFM) and the evolution of the recrystallization of the amorphized layers and the removal of the defects by means of cross-section Transmission Electron Microscopy.

Local control of spin polarization in a semiconductor by microscale current loops

We demonstrate a method to electrically manipulate the spin polarization in a semiconductor on a micrometer length scale and a submicrosecond time scale. A variable magnetic field induced by a microscale current loop magnetizes the Mn2+ ions in a CdMnTe/CdMgTe diluted magnetic semiconductor quantum well, and via sp-d exchange interaction polarizes photogenerated electron-hole pairs. A maximum spin polarization degree of ±8.5% is obtained at 4.2 K without external magnetic field. The induced carrier spin polarization and the thermal heating of Mn2+ spins are resolved spatially and temporally by microphotoluminescence measurements.

Effects of pH on the peripheral light-harvesting antenna complex for Rhodopseudomonas palustris

In this work steady-state absorption spectroscopy, circular dichroism spectroscopy and sub-microsecond time-resolved absorption spectroscopy were used to investigate the effect of pH on the structures and functions of LH2 complex for Rhodopseudomonas palustris. The results revealed that: (1) B800 Bchla was gradually transformed to free pigments absorbing around 760 nm on the minutes timescale upon the induction of strong acidic pH, and subsequently there disappeared the CD signal for Q(y) band of B800 in the absence of B800. In addition, Carotenoids changed with the similar tendency to B850 BChl. (2) The introduction of strong basic pH gave rise to no significant changes for B800 Bchla, while B850 BChla experienced remarkable spectral blue-shift from 852 to 837 nm. Similar phenomenon was seen for the CD signal for Q(y) band of B850. Carotenoids displayed strong and pH-independent CD signals in the visible range. (3) In the case of both physiological and basic pH, broad and asymmetrical positive T( n ) <-- T(1) transient absorption appeared following the pulsed photo-excitation of Car at 532 nm. By contrast, the featureless and weak positive signal was observed on the sub-microsecond timescale in the acidic pH environment. The aforementioned experimental results indicated that acidic pH-induced removal of B800 Bchla prevented the generation of the carotenoid triplet state ((3)Car), which is known to be essential for the photo-protection function. Nevertheless, carotenoids can still perform this important physiological role under the basic pH condition, where the spectral blue shift of B850 exerts little effect on the overall structure of the cyclic aggregate, therefore favoring the formation of carotenoid triplet state.

Piezoresponse Force Microscopy Studies of Switching Behavior of Ferroelectric Capacitors on a 100-ns Time Scale

Piezoresponse force microscopy is a powerful technique for nm-scale studies but is usually limited by response time. In this Letter, we report the first direct studies of ferroelectric capacitor switching on a submicrosecond time scale. Simultaneous domain imaging and sub-mus transient current measurements establish a direct relationship between polarization P(t) and domain kinetics. Switching times scale with capacitor size over an order of magnitude. Small capacitors, where polarization reversal is dominated by domain wall motion, switch faster at high fields but more slowly at low fields while larger capacitors do the reverse.