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Sökning: WFRF:(Pomorski M) > (2017)

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1.
  • Janiak, M., et al. (författare)
  • β -delayed proton emission from P 26 and S 27
  • 2017
  • Ingår i: Physical Review C: covering nuclear physics. - 2469-9985. ; 95:3
  • Tidskriftsartikel (refereegranskat)abstract
    • Delayed emission of protons following β decay of neutron deficient nuclei P26 and S27 was investigated at the ACCULINNA separator in the Flerov Laboratory of Nuclear Reactions at Dubna. Ions of interest, identified in flight, were implanted into the active volume of the gaseous optical time projection chamber, which allowed us to record tracks of charged particles emitted in the decay. Total branching ratios for β-delayed proton emission and for β-delayed two-proton emission were determined. In addition, energy spectra for delayed protons below 2 MeV were established. Our findings for P26 agree with results of previous experiments. In the case of S27, however, the observed probability of delayed proton emission is an order of magnitude larger than reported in literature. Two new strong proton transitions were identified representing decays of the first two excited states of P27 to the ground state of Si26. The probability ratio of γ-to-proton emission from these states is discussed.
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3.
  • Jensen, M. S., et al. (författare)
  • Phospholipid flipping involves a central cavity in P4 ATPases
  • 2017
  • Ingår i: Scientific Reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 7:1
  • Tidskriftsartikel (refereegranskat)abstract
    • P4 ATPase flippases translocate phospholipids across biomembranes, thus contributing to the establishment of transmembrane lipid asymmetry, a feature important for multiple cellular processes. The mechanism by which such phospholipid flipping occurs remains elusive as P4 ATPases transport a giant substrate very different from that of other P-type ATPases such as Na+/K+-and Ca2+-ATPases. Based on available crystal structures of cation-transporting P-type ATPases, we generated a structural model of the broad-specificity flippase ALA10. In this model, a cavity delimited by transmembrane segments TM3, TM4, and TM5 is present in the transmembrane domain at a similar position as the cation-binding region in related P-type ATPases. Docking of a phosphatidylcholine headgroup in silico showed that the cavity can accommodate a phospholipid headgroup, likely leaving the fatty acid tails in contact with the hydrophobic portion of the lipid bilayer. Mutagenesis data support this interpretation and suggests that two residues in TM4 (Y374 and F375) are important for coordination of the phospholipid headgroup. Our results point to a general mechanism of lipid translocation by P4 ATPases, which closely resembles that of cation-transporting pumps, through coordination of the hydrophilic portion of the substrate in a central membrane cavity.
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  • Resultat 1-3 av 3

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