13 research outputs found

    Spectroscopy of 18^{18}Na: Bridging the two-proton radioactivity of 19^{19}Mg

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    The unbound nucleus 18^{18}Na, the intermediate nucleus in the two-proton radioactivity of 19^{19}Mg, was studied by the measurement of the resonant elastic scattering reaction 17^{17}Ne(p,17^{17}Ne)p performed at 4 A.MeV. Spectroscopic properties of the low-lying states were obtained in a R-matrix analysis of the excitation function. Using these new results, we show that the lifetime of the 19^{19}Mg radioactivity can be understood assuming a sequential emission of two protons via low energy tails of 18^{18}Na resonances

    Spectroscopy of the unbound nucleus 18Na

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    Expérience GANIL, SPIRALInternational audienceThe unbound nucleus 18Na, the intermediate nucleus in the two-proton radioactivity of 19Mg, is studied through the resonant elastic scattering 17Ne(p,17Ne)p. The spectroscopic information obtained in this experiment is discussed and put in perspective with previous measurements and the structure of the mirror nucleus 18N

    The Role of UPF0157 in the Folding of M. tuberculosis Dephosphocoenzyme A Kinase and the Regulation of the Latter by CTP

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    BACKGROUND:Targeting the biosynthetic pathway of Coenzyme A (CoA) for drug development will compromise multiple cellular functions of the tubercular pathogen simultaneously. Structural divergence in the organization of the penultimate and final enzymes of CoA biosynthesis in the host and pathogen and the differences in their regulation mark out the final enzyme, dephosphocoenzyme A kinase (CoaE) as a potential drug target. METHODOLOGY/PRINCIPAL FINDINGS:We report here a complete biochemical and biophysical characterization of the M. tuberculosis CoaE, an enzyme essential for the pathogen's survival, elucidating for the first time the interactions of a dephosphocoenzyme A kinase with its substrates, dephosphocoenzyme A and ATP; its product, CoA and an intrinsic yet novel inhibitor, CTP, which helps modulate the enzyme's kinetic capabilities providing interesting insights into the regulation of CoaE activity. We show that the mycobacterial enzyme is almost 21 times more catalytically proficient than its counterparts in other prokaryotes. ITC measurements illustrate that the enzyme follows an ordered mechanism of substrate addition with DCoA as the leading substrate and ATP following in tow. Kinetic and ITC experiments demonstrate that though CTP binds strongly to the enzyme, it is unable to participate in DCoA phosphorylation. We report that CTP actually inhibits the enzyme by decreasing its Vmax. Not surprisingly, a structural homology search for the modeled mycobacterial CoaE picks up cytidylmonophosphate kinases, deoxycytidine kinases, and cytidylate kinases as close homologs. Docking of DCoA and CTP to CoaE shows that both ligands bind at the same site, their interactions being stabilized by 26 and 28 hydrogen bonds respectively. We have also assigned a role for the universal Unknown Protein Family 0157 (UPF0157) domain in the mycobacterial CoaE in the proper folding of the full length enzyme. CONCLUSIONS/SIGNIFICANCE:In view of the evidence presented, it is imperative to assign a greater role to the last enzyme of Coenzyme A biosynthesis in metabolite flow regulation through this critical biosynthetic pathway

    Beta Decay of 82^{82}Ga Studied at the ALTO Facility

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    International audienceExcited states in the N = 50 nucleus 82Ge have been investigated via beta decay of 82Ga at the ALTO facility. More than 50 new gamma transitions were identified. The preliminary results are presented in this work

    Spectroscopy of the unbound nucleus <sup>18</sup>Na

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    The unbound nucleus 18Na, the intermediate nucleus in the two-proton radioactivity of 19Mg, is studied through the resonant elastic scattering 17Ne(p,17Ne)p. The spectroscopic information obtained in this experiment is discussed and put in perspective with previous measurements and the structure of the mirror nucleus 18N. © 2011 World Scientific Publishing Company

    Spectroscopy of 18^{18}Na: Bridging the two-proton radioactivity of 19^{19}Mg

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    The unbound nucleus 18^{18}Na, the intermediate nucleus in the two-proton radioactivity of 19^{19}Mg, was studied by the measurement of the resonant elastic scattering reaction 17^{17}Ne(p,17^{17}Ne)p performed at 4 A.MeV. Spectroscopic properties of the low-lying states were obtained in a R-matrix analysis of the excitation function. Using these new results, we show that the lifetime of the 19^{19}Mg radioactivity can be understood assuming a sequential emission of two protons via low energy tails of 18^{18}Na resonances

    Spectroscopy of the Unbound Nucleus Na-18

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    The unbound nucleus Na-18, the intermediate nucleus in the two-proton radioactivity of Mg-19 is studied through the resonant elastic scattering Ne-17(p,Ne-17)p. The spectroscopic information obtained in this experiment is discussed and put in perspective with previous measurements and the structure of the mirror nucleus N-18.2nd Workshop on State of the Art in Nuclear Cluster Physics, May 25-28, 2010, Univ Libre Brussels, Brussels, Belgiu

    Submarine landslides at the eastern Sunda margin: observations and tsunami impact assessment

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    Our analysis of new bathymetric data reveals six submarine landslides at the eastern Sunda margin between central Java and Sumba Island, Indonesia. Their volumes range between 1 km³ in the Java fore-arc basin up to 20 km³ at the trench off Sumba and Sumbawa. We estimate the potential hazard of each event by modeling the corresponding tsunami and its run-up on nearby coasts. Four slides are situated remarkably close to the epicenter of the 1977 tsunamigenic Sumba M w = 8.3 earthquake. However, comparison of documented tsunami run-up heights and arrival times with our modeling results neither allows us to confirm nor can we falsify the hypothesis that the earthquake triggered these submarine landslides
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