Enhancing the critical current in quasiperiodic pinning arrays below and above the matching magnetic flux

Quasiperiodic pinning arrays, as recently demonstrated theoretically and experimentally using a five-fold Penrose tiling, can lead to a significant enhancement of the critical current Ic as compared to "traditional" regular pinning arrays. However, while regular arrays showed only a sharp peak in Ic(Phi) at the matching flux Phi1 and quasiperiodic arrays provided a much broader maximum at Phi<Phi1, both types of pinning arrays turned out to be inefficient for fluxes larger than Phi1. We demonstrate theoretically and experimentally the enhancement of Ic(Phi) for Phi>Phi1 by using non-Penrose quasiperiodic pinning arrays. This result is based on a qualitatively different mechanism of flux pinning by quasiperiodic pinning arrays and could be potentially useful for applications in superconducting micro-electronic devices operating in a broad range of magnetic fields.Comment: 7 pages, 4 figure

Suppression of dissipation in Nb thin films with triangular antidot arrays by random removal of pinning sites

The depinning current Ic versus applied magnetic field B close to the transition temperature Tc of Nb thin films with randomly diluted triangular arrays of antidots is investigated. % Our experiments confirm essential features in Ic(B) as predicted by Reichhardt and Olson Reichhardt [Phys.Rev. B 76, 094512 (2007)]. % We show that, by introducing disorder into periodic pinning arrays, Ic can be enhanced. % In particular, for arrays with fixed density n_p of antidots, an increase in dilution Pd induces an increase in Ic and decrease of the flux-flow voltage for B>Bp=n_p Phi_0.Comment: 5 pages, 4 figure

Bimodal Phase Diagram of the Superfluid Density in LaAlO3/SrTiO3 Revealed by an Interfacial Waveguide Resonator

We explore the superconducting phase diagram of the two-dimensional electron system at the LaAlO3/SrTiO3 interface by monitoring the frequencies of the cavity modes of a coplanar waveguide resonator fabricated in the interface itself. We determine the phase diagram of the superconducting transition as a function of temperature and electrostatic gating, finding that both the superfluid density and the transition temperature follow a dome shape, but that the two are not monotonically related. The ground state of this 2DES is interpreted as a Josephson junction array, where a transition from long- to short-range order occurs as a function of the electronic doping. The synergy between correlated oxides and superconducting circuits is revealed to be a promising route to investigate these exotic compounds, complementary to standard magneto-transport measurements.Comment: 5 pages, 4 figures and 10 pages of supplementary materia

Rotavirus infection activates the UPR but modulates its activity

<p>Abstract</p> <p>Background</p> <p>Rotaviruses are known to modulate the innate antiviral defense response driven by IFN. The purpose of this study was to identify changes in the cellular proteome in response to rotavirus infection in the context of the IFN response. We also sought to identify proteins outside the IFN induction and signaling pathway that were modulated by rotavirus infection.</p> <p>Methods</p> <p>2D-DIGE and image analysis were used to identify cellular proteins that changed in levels of expression in response to rotavirus infection, IFN treatment, or IFN treatment prior to infection. Immunofluorescence microscopy was used to determine the subcellular localization of proteins associated with the unfolded protein response (UPR).</p> <p>Results</p> <p>The data show changes in the levels of multiple proteins associated with cellular stress in infected cells, including levels of ER chaperones GRP78 and GRP94. Further investigations showed that GRP78, GRP94 and other proteins with roles in the ER-initiated UPR including PERK, CHOP and GADD34, were localized to viroplasms in infected cells.</p> <p>Conclusions</p> <p>Together the results suggest rotavirus infection activates the UPR, but modulates its effects by sequestering sensor, transcription factor, and effector proteins in viroplasms. The data consequently also suggest that viroplasms may directly or indirectly play a fundamental role in regulating signaling pathways associated with cellular defense responses.</p

Evidence That the P\u3csub\u3ei\u3c/sub\u3e Release Event Is the Rate-Limiting Step in the Nitrogenase Catalytic Cycle

Nitrogenase reduction of dinitrogen (N2) to ammonia (NH3) involves a sequence of events that occur upon the transient association of the reduced Fe protein containing two ATP molecules with the MoFe protein that includes electron transfer, ATP hydrolysis, Pi release, and dissociation of the oxidized, ADP-containing Fe protein from the reduced MoFe protein. Numerous kinetic studies using the nonphysiological electron donor dithionite have suggested that the rate-limiting step in this reaction cycle is the dissociation of the Fe protein from the MoFe protein. Here, we have established the rate constants for each of the key steps in the catalytic cycle using the physiological reductant flavodoxin protein in its hydroquinone state. The findings indicate that with this reductant, the rate-limiting step in the reaction cycle is not protein–protein dissociation or reduction of the oxidized Fe protein, but rather events associated with the Pi release step. Further, it is demonstrated that (i) Fe protein transfers only one electron to MoFe protein in each Fe protein cycle coupled with hydrolysis of two ATP molecules, (ii) the oxidized Fe protein is not reduced when bound to MoFe protein, and (iii) the Fe protein interacts with flavodoxin using the same binding interface that is used with the MoFe protein. These findings allow a revision of the rate-limiting step in the nitrogenase Fe protein cycle

The Nucleotide Exchange Factor Ric-8A is a Chaperone for the Conformationally Dynamic Nucleotide-Free State of G Alpha I1

Heterotrimeric G protein alpha subunits are activated upon exchange of GDP for GTP at the nucleotide binding site of G alpha, catalyzed by guanine nucleotide exchange factors (GEFs). In addition to transmembrane G protein-coupled receptors (GPCRs), which act on G protein heterotrimers, members of the family cytosolic proteins typified by mammalian Ric-8A are GEFs for Gi/q/12/13-class G alpha subunits. Ric-8A binds to G alpha.GDP, resulting in the release of GDP. The Ric-8A complex with nucleotide-free G alpha i1 is stable, but dissociates upon binding of GTP to G alpha i1. To gain insight into the mechanism of Ric-8A-catalyzed GDP release from G alpha i1, experiments were conducted to characterize the physical state of nucleotide-free G alpha i1 (hereafter referred to as G alpha i1[]) in solution, both as a monomeric species, and in the complex with Ric-8A. We found that Ric-8A-bound, nucleotide-free G alpha i1 is more accessible to trypsinolysis than G alpha i1.GDP, but less so than G alpha i1[] alone. The TROSY-HSQC spectrum of [N-15]G alpha i1[] bound to Ric-8A shows considerable loss of peak intensity relative to that of [N-15]G alpha i1.GDP. Hydrogen-deuterium exchange in G alpha i1[] bound to Ric-8A is 1.5-fold more extensive than in G alpha i1.GDP. Differential scanning calorimetry shows that both Ric-8A and G alpha i1.GDP undergo cooperative, irreversible unfolding transitions at 47 degrees and 52 degrees, respectively, while nucleotide-free G alpha i1 shows a broad, weak transition near 35 degrees. The unfolding transition for Ric-8A: G alpha i1[] is complex, with a broad transition that peaks at 50 degrees, suggesting that both Ric-8A and G alpha i1[] are stabilized within the complex, relative to their respective free states. The C-terminus of G alpha i1 is shown to be a critical binding element for Ric-8A, as is also the case for GPCRs, suggesting that the two types of GEF might promote nucleotide exchange by similar mechanisms, by acting as chaperones for the unstable and dynamic nucleotide-free state of G alpha