Radio Images of 3C 58: Expansion and Motion of its Wisp

New 1.4 GHz VLA observations of the pulsar-powered supernova remnant 3C 58 have resulted in the highest-quality radio images of this object to date. The images show filamentary structure over the body of the nebula. The present observations were combined with earlier ones from 1984 and 1991 to investigate the variability of the radio emission on a variety of time-scales. No significant changes are seen over a 110 day interval. In particular, the upper limit on the apparent projected velocity of the wisp is 0.05c. The expansion rate of the radio nebula was determined between 1984 and 2004, and is 0.014+/-0.003%/year, corresponding to a velocity of 630+/-70 km/s along the major axis. If 3C 58 is the remnant of SN 1181, it must have been strongly decelerated, which is unlikely given the absence of emission from the supernova shell. Alternatively, the low expansion speed and a number of other arguments suggest that 3C 58 may be several thousand years old and not be the remnant of SN 1181.Comment: 12 pages; accepted for publication in the Astrophysical Journa

Four-quark flux distribution and binding in lattice SU(2)

The full spatial distribution of the color fields of two and four static quarks is measured in lattice SU(2) field theory at separations up to 1 fm at beta=2.4. The four-quark case is equivalent to a qbar q qbar q system in SU(2) and is relevant to meson-meson interactions. By subtracting two-body flux tubes from the four-quark distribution we isolate the flux contribution connected with the four-body binding energy. This contribution is further studied using a model for the binding energies. Lattice sum rules for two and four quarks are used to verify the results.Comment: 46 pages including 71 eps figures. 3D color figures are available at www.physics.helsinki.fi/~ppennane/pics

Charge shelving and bias spectroscopy for the readout of a charge-qubit on the basis of superposition states

Charge-based qubits have been proposed as fundamental elements for quantum computers. One commonly proposed readout device is the single-electron transistor (SET). SETs can distinguish between localized charge states, but lack the sensitivity to directly distinguish superposition states, which have greatly enhanced coherence times compared with position states. We propose introducing a third dot, and exploiting energy dependent tunnelling from the qubit into this dot (bias spectroscopy) for pseudo-spin to charge conversion and superposition basis readout. We introduce an adiabatic fast passage-style charge pumping technique which enables efficient and robust readout via charge shelving, avoiding problems due to finite SET measurement time.Comment: 4 pages, 3 figures, note slightly changed title, replaced with journal versio

Identification of the YfgF MASE1 domain as a modulator of bacterial responses to aspartate

Complex 3'-5'-cyclic diguanylic acid (c-di-GMP) responsive regulatory networks that are modulated by the action of multiple diguanylate cyclases (DGC; GGDEF domain proteins) and phosphodiesterases (PDE; EAL domain proteins) have evolved in many bacteria. YfgF proteins possess a membrane-anchoring domain (MASE1), a catalytically inactive GGDEF domain and a catalytically active EAL domain. Here, sustained expression of the Salmonella enterica spp. Enterica ser. Enteritidis YfgF protein is shown to mediate inhibition of the formation of the aspartate chemotactic ring on motility agar under aerobic conditions. This phenomenon was c-di-GMP-independent because it occurred in a Salmonella strain that lacked the ability to synthesize c-di-GMP and also when PDE activity was abolished by site-directed mutagenesis of the EAL domain. YfgF-mediated inhibition of aspartate chemotactic ring formation was impaired in the altered redox environment generated by exogenous p-benzoquinone. This ability of YfgF to inhibit the response to aspartate required a motif, (213)Lys-Lys-Glu(215), in the predicted cytoplasmic loop between trans-membrane regions 5 and 6 of the MASE1 domain. Thus, for the first time the function of a MASE1 domain as a redox-responsive regulator of bacterial responses to aspartate has been shown