Probing the messenger of supersymmetry breaking by the muon anomalous magnetic moment

Motivated by the recently measured muon's anomalous magnetic moment $a_{\mu}$, we examine the supersymmetry contribution to $a_{\mu}$ in various mediation models of supersymmetry breaking which lead to predictive flavor conserving soft parameters at high energy scale. The studied models include dilaton/modulus-mediated models in heterotic string/$M$ theory, gauge-mediated model, no-scale or gaugino-mediated model, and also the minimal and deflected anomaly-mediated models. For each model, the range of $a^{SUSY}_{\mu}$ allowed by other experimental constraints, e.g. b --> s\gamma and the collider bounds on superparticle masses, is obtained together with the corresponding parameter region of the model. Gauge-mediated models with low messenger scale can give any $a^{SUSY}_{\mu}$ within the $2\sigma$ bound. In many other models, b --> s\gamma favors $a^{SUSY}_{\mu}$ smaller than either the $-1\sigma$ value ($26\times 10^{-10}$) or the central value ($42\times 10^{-10}$).Comment: RevTeX, 29 pages, 14 eps figures, figure for deflected anomaly mediation is corrected, reference adde

Histidine 454 plays an important role in polymerization of human glutamate dehydrogenase

AbstractAlthough previous chemical modification studies have suggested several residues to be involved in the maintenance of the quaternary structure of glutamate dehydrogenase (GDH), there are conflicting views for the polymerization process and no clear evidence has been reported yet. In the present study, cassette mutagenesis at seven putative positions (Lys333, Lys337, Lys344, Lys346, Ser445, Gly446, and His454) was performed using a synthetic human GDH gene to examine the polymerization process. Of the mutations at the seven different sites, only the mutagenesis at His454 results in depolymerization of the hexameric GDH into active trimers as determined by HPLC gel filtration analysis and native gradient polyacrylamide gel electrophoresis. The mutagenesis at His454 has no effects on expression or stability of the protein. The KM values for NADH and 2-oxoglutarate were 1.5-fold and 2.5-fold greater, respectively, for the mutant GDH than for wild-type GDH, indicating that substitution at position 454 had appreciable effects on the affinity of the enzyme for both NADH and 2-oxoglutarate. The Vmax values were similar for wild-type and mutant GDH. The kcat/KM value of the mutant GDH was reduced up to 2.8-fold. The decreased efficiency of the mutant, therefore, results from the increase in KM values for NADH and 2-oxoglutarate. The results with cassette mutagenesis and HPLC gel filtration analysis suggest that His454 is involved in the polymerization process of human GDH

Light cold dark matter from non-thermal decay

We investigate the mass range and the corresponding free-streaming length scale of dark matter produced non-thermally from decay of heavy objects which can be either dominant or sub-dominant at the moment of decay. We show that the resulting dark matter could be very light well below keV scale with a free-streaming length satisfying the Lyman-{\alpha} constraints. We demonstrate two explicit examples for such light cold dark matter.Comment: 8 pages, 4 figure