Simultaneous dynamic characterization of charge and structural motion during ferroelectric switching

Monitoring structural changes in ferroelectric thin films during electric field-induced polarization switching is important for a full microscopic understanding of the coupled motion of charges, atoms and domain walls. We combine standard ferroelectric test-cycles with time-resolved x-ray diffraction to investigate the response of a nanoscale ferroelectric oxide capacitor upon charging, discharging and switching. Piezoelectric strain develops during the electronic RC time constant and additionally during structural domain-wall creep. The complex atomic motion during ferroelectric polarization reversal starts with a negative piezoelectric response to the charge flow triggered by voltage pulses. Incomplete screening limits the compressive strain. The piezoelectric modulation of the unit cell tweaks the energy barrier between the two polarization states. Domain wall motion is evidenced by a broadening of the in-plane components of Bragg reflections. Such simultaneous measurements on a working device elucidate and visualize the complex interplay of charge flow and structural motion and challenges theoretical modelling

Dynamical response and confinement of the electrons at the LaAlO3/SrTiO3 interface

With infrared ellipsometry and transport measurements we investigated the electrons at the interface between LaAlO3 and SrTiO3. We obtained a sheet carrier density of Ns~5-9x 10E13 cm^-2, an effective mass of m*~3m_e, and a strongly frequency dependent mobility. The latter are similar as in bulk SrTi1-xNbxO3 and therefore suggestive of polaronic correlations of the confined carriers. We also determined the vertical density profile which has a strongly asymmetric shape with a rapid initial decay over the first 2 nm and a pronounced tail that extends to about 11 nm.Comment: 4 pages, 3 figures, 1 EPAPS file (3 figures

Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths

At a resting sarcomere length of approximately 2.2 µm bony fish muscles put into rigor in the presence of BDM (2,3-butanedione monoxime) to reduce rigor tension generation show the normal arrangement of myosin head interactions with actin filaments as monitored by low-angle X-ray diffraction. However, if the muscles are put into rigor using the same protocol but stretched to 2.5 µm sarcomere length, a markedly different structure is observed. The X-ray diffraction pattern is not just a weaker version of the pattern at full overlap, as might be expected, but it is quite different. It is compatible with the actin-attached myosin heads being in a different conformation on actin, with the average centre of cross-bridge mass at a higher radius than in normal rigor and the myosin lever arms conforming less to the actin filament geometry, probably pointing back to their origins on their parent myosin filaments. The possible nature of this new rigor cross-bridge conformation is discussed in terms of other well-known states such as the weak binding state and the ‘roll and lock’ mechanism; we speculate that we may have trapped most myosin heads in an early attached strong actin-binding state in the cross-bridge cycle on actin

Strong binding of myosin heads stretches and twists the actin helix

AbstractCalculation of the size of the power stroke of the myosin motor in contracting muscle requires knowledge of the compliance of the myofilaments. Current estimates of actin compliance vary significantly introducing uncertainty in the mechanical parameters of the motor. Using x-ray diffraction on small bundles of permeabilized fibers from rabbit muscle we show that strong binding of myosin heads changes directly the actin helix. The spacing of the 2.73-nm meridional x-ray reflection increased by 0.22% when relaxed fibers were put into low-tension rigor (<10kN/m2) demonstrating that strongly bound myosin heads elongate the actin filaments even in the absence of external tension. The pitch of the 5.9-nm actin layer line increased by ∼0.62% and that of the 5.1-nm layer line decreased by ∼0.26%, suggesting that the elongation is accompanied by a decrease in its helical angle (∼166°) by ∼0.8°. This effect explains the difference between actin compliance revealed from mechanical experiments with single fibers and from x-ray diffraction on whole muscles. Our measurement of actin compliance obtained by applying tension to fibers in rigor is consistent with the results of mechanical measurements

The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron–electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a ‘self-chaperoning’ type mechanism

Flexibility of KorA, a plasmid-encoded, global transcription regulator, in the presence and the absence of its operator

The IncP (Incompatibility group P) plasmids are important carriers in the spread of antibiotic resistance across Gram-negative bacteria. Gene expression in the IncP-1 plasmids is stringently controlled by a network of four global repressors, KorA, KorB, TrbA and KorC interacting cooperatively. Intriguingly, KorA and KorB can act as co-repressors at varying distances between their operators, even when they are moved to be on opposite sides of the DNA. KorA is a homodimer with the 101-amino acid subunits, folding into an N-terminal DNA-binding domain and a C-terminal dimerization domain. In this study, we have determined the structures of the free KorA repressor and two complexes each bound to a 20-bp palindromic DNA duplex containing its consensus operator sequence. Using a combination of X-ray crystallography, nuclear magnetic resonance spectroscopy, SAXS and molecular dynamics calculations, we show that the linker between the two domains is very flexible and the protein remains highly mobile in the presence of DNA. This flexibility allows the DNA-binding domains of the dimer to straddle the operator DNA on binding and is likely to be important in cooperative binding to KorB. Unexpectedly, the C-terminal domain of KorA is structurally similar to the dimerization domain of the tumour suppressor p53

Angular dependence of resistivity in the superconducting state of NdFeAsO0.82_{0.82}F0.18_{0.18} single crystals

We report the results of angle dependent resistivity of NdFeAsO$_{0.82}$F$_{0.18}$ single crystals in the superconducting state. By doing the scaling of resistivity within the frame of the anisotropic Ginzburg-Landau theory, it is found that the angle dependent resistivity measured under different magnetic fields at a certain temperature can be collapsed onto one curve. As a scaling parameter, the anisotropy $\Gamma$ can be determined for different temperatures. It is found that $\Gamma(T)$ increases slowly with decreasing temperature, varying from $\Gamma \simeq$ 5.48 at T=50 K to $\Gamma \simeq$ 6.24 at T=44 K. This temperature dependence can be understood within the picture of multi-band superconductivity.Comment: 7 pages, 4 figure