Electrical and optical properties of fluid iron from compressed to expanded regime

Using quantum molecular dynamics simulations, we show that the electrical and optical properties of fluid iron change drastically from compressed to expanded regime. The simulation results reproduce the main trends of the electrical resistivity along isochores and are found to be in good agreement with experimental data. The transition of expanded fluid iron into a nonmetallic state takes place close to the density at which the constant volume derivative of the electrical resistivity on internal energy becomes negative. The study of the optical conductivity, absorption coefficient, and Rosseland mean opacity shows that, quantum molecular dynamics combined with the Kubo-Greenwood formulation provides a powerful tool to calculate and benchmark the electrical and optical properties of iron from expanded fluid to warm dense region

The Υ(1S)\Upsilon(1S) leptonic decay using the principle of maximum conformality

In the paper, we study the $\Upsilon(1S)$ leptonic decay width $\Gamma(\Upsilon(1S)\to \ell^+\ell^-)$ by using the principle of maximum conformality (PMC) scale-setting approach. The PMC adopts the renormalization group equation to set the correct momentum flow of the process, whose value is independent to the choice of the renormalization scale and its prediction thus avoids the conventional renormalization scale ambiguities. Using the known next-to-next-to-next-to-leading order perturbative series together with the PMC single scale-setting approach, we do obtain a renormalization scale independent decay width, $\Gamma_{\Upsilon(1S) \to e^+ e^-} = 1.262^{+0.195}_{-0.175}$ keV, where the error is squared average of those from $\alpha_s(M_{Z})=0.1181\pm0.0011$, $m_b=4.93\pm0.03$ GeV and the choices of factorization scales within $\pm 10\%$ of their central values. To compare with the result under conventional scale-setting approach, this decay width agrees with the experimental value within errors, indicating the importance of a proper scale-setting approach.Comment: 6 pages, 4 figure

Genome-wide comparative analysis of metacaspases in unicellular and filamentous cyanobacteria

<p>Abstract</p> <p>Background</p> <p>Cyanobacteria are an ancient group of photoautotrophic prokaryotes with wide variations in genome size and ecological habitat. Metacaspases (MCAs) are cysteine proteinases that have sequence homology to caspases and play essential roles in programmed cell death (PCD). MCAs have been identified in several prokaryotes, fungi and plants; however, knowledge about cyanobacterial metacaspases still remains obscure. With the availability of sequenced genomes of 33 cyanobacteria, we perform a comparative analysis of metacaspases and explore their distribution, domain structure and evolution.</p> <p>Results</p> <p>A total of 58 putative MCAs were identified, which are abundant in filamentous diazotrophic cyanobacteria and <it>Acaryochloris marina </it>MBIC 11017 and absent in all <it>Prochlorococcus </it>and marine <it>Synechococcus </it>strains, except <it>Synechococcus </it>sp. PCC 7002. The Cys-His dyad of caspase superfamily is conserved, while mutations (Tyr in place of His and Ser/Asn/Gln/Gly instead of Cys) are also detected in some cyanobacteria. MCAs can be classified into two major families (α and β) based on the additional domain structure. Ten types and a total of 276 additional domains were identified, most of which involves in signal transduction. Apoptotic related NACHT domain was also found in two cyanobacterial MCAs. Phylogenetic tree of MCA catalytic P20 domains coincides well with the domain structure and the phylogenies based on 16s rRNA.</p> <p>Conclusions</p> <p>The existence and quantity of MCA genes in unicellular and filamentous cyanobacteria are a function of the genome size and ecological habitat. MCAs of family α and β seem to evolve separately and the recruitment of WD40 additional domain occurs later than the divergence of the two families. In this study, a general framework of sequence-structure-function connections for the metacaspases has been revealed, which may provide new targets for function investigation.</p