Relationship of self-focusing to spatial instability modes

The spatial distribution of focal spots formed when laser beams self- focus in materials is shown to originate from the growth of certain instability modes. These modes are determined by a simple mathematical relationship derived from instability theory, which has been verified experimentally. Because of these instabilities, the threshold power for self-focusing is inversely proportional to the self-focusing length for high-power laser beams. (auth

Resistive g-modes in a reversed field pinch plasma

First direct experimental evidence of high frequency, high toroidal mode number (n>20), magnetic fluctuations due to unstable resistive interchange modes (g-modes) resonant in the edge region of a reversed field pinch (RFP) plasma is presented. Experimental characterization of time and space periodicities of the modes is provided by means of highly resolved in-vessel edge and insertable magnetic diagnostics. It is found that the spectral mode properties are in good agreement with the predictions of the theoretical linear resistive magnetohydrodynamic stability analysis. A simple model is proposed for the observed saturation levels of the modes.Comment: Submitted to Physical Review Letter

Magnetic Phase transitions in Plasmas and Transport Barriers

A model of magnetic phase transitions in plasmas is presented: plasma blobs with pressure excess or defect are dia- or para-magnets and move radially under the influence of the background plasma magnetisation. It is found that magnetic phase separation could be the underlying mechanism of L to H transitions and drive transport barrier formation. Magnetic phase separation and associated pedestal build up, as described here, can be explained by the well known interchange mechanism, now reinterpreted as a magnetisation interchange which remains relevant even when stable or saturated. A testable necessary criterion for the L to H transition is presented.Comment: 3 figures, 9 pages, equations created with MathType To be published in Nuclear Fusion, accepted August 201

Biochemical, Structural and Molecular Dynamics Analyses of the Potential Virulence Factor RipA from Yersinia pestis

Human diseases are attributed in part to the ability of pathogens to evade the eukaryotic immune systems. A subset of these pathogens has developed mechanisms to survive in human macrophages. Yersinia pestis, the causative agent of the bubonic plague, is a predominately extracellular pathogen with the ability to survive and replicate intracellularly. A previous study has shown that a novel rip (required for intracellular proliferation) operon (ripA, ripB and ripC) is essential for replication and survival of Y. pestis in postactivated macrophages, by playing a role in lowering macrophage-produced nitric oxide (NO) levels. A bioinformatics analysis indicates that the rip operon is conserved among a distally related subset of macrophage-residing pathogens, including Burkholderia and Salmonella species, and suggests that this previously uncharacterized pathway is also required for intracellular survival of these pathogens. The focus of this study is ripA, which encodes for a protein highly homologous to 4-hydroxybutyrate-CoA transferase; however, biochemical analysis suggests that RipA functions as a butyryl-CoA transferase. The 1.9 Å X-ray crystal structure reveals that RipA belongs to the class of Family I CoA transferases and exhibits a unique tetrameric state. Molecular dynamics simulations are consistent with RipA tetramer formation and suggest a possible gating mechanism for CoA binding mediated by Val227. Together, our structural characterization and molecular dynamic simulations offer insights into acyl-CoA specificity within the active site binding pocket, and support biochemical results that RipA is a butyryl-CoA transferase. We hypothesize that the end product of the rip operon is butyrate, a known anti-inflammatory, which has been shown to lower NO levels in macrophages. Thus, the results of this molecular study of Y. pestis RipA provide a structural platform for rational inhibitor design, which may lead to a greater understanding of the role of RipA in this unique virulence pathway