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Sökning: WFRF:(Gomi H)

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  • Shimoura, S., et al. (författare)
  • Lifetime of the isomeric O-2(+) state in Be-12
  • 2007
  • Ingår i: Physics Letters. Section B: Nuclear, Elementary Particle and High-Energy Physics. - : Elsevier BV. - 0370-2693. ; 654:3-4, s. 87-91
  • Tidskriftsartikel (refereegranskat)abstract
    • Mean lifetime tau of the isomeric O-2(+) state in Be-12 has been determined by measuring decay spectra of delayed y-rays from stopped Be-12 2 nuclei produced by the projectile fragmentation of O-18 at 100 A MeV. A consistent value of tau = 331 +/- 12 ns was obtained from the time spectra of the E2 gamma decay to the 2(1)(+) state and the positron annihilation following the E0 decay to the ground state. Based on the observed branching ratio between the E2 and E0 decays, transition strengths of the two decay modes were deduced to be B(E2; O-2(+) -> 2(1)(+)) = 7.0 +/- 0.6 e(2) fm(4) and 2 1 1 (O-2(+) Sigma(i) e(i) r(i)(2) O-1(+)), = 0.87 +/- 0.03 e fM(2), respectively. (C) 2007 Elsevier B.V. All rights reserved.
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  • Frick, Inga-Maria, et al. (författare)
  • Convergent evolution among immunoglobulin G-binding bacterial proteins
  • 1992
  • Ingår i: Proceedings of the National Academy of Sciences. - 1091-6490. ; 89:18, s. 8532-8536
  • Tidskriftsartikel (refereegranskat)abstract
    • Protein G, a bacterial cell-wall protein with high affinity for the constant region of IgG (IgGFc) antibodies, contains homologous repeats responsible for the interaction with IgGFc. A synthetic peptide corresponding to an 11-amino acid-long sequence in the COOH-terminal region of the repeats was found to bind to IgGFc and block the interaction with protein G. Moreover, two other IgGFc-binding bacterial proteins (proteins A and H), which do not contain any sequences homologous to the peptide, were also inhibited in their interactions with IgGFc by the peptide. Finally, a decapeptide based on a sequence in IgGFc blocked the binding of all three proteins to IgGFc. This unusually clear example of convergent evolution emphasizes the complexity of protein-protein interactions and suggests that bacterial surface-protein interaction with host protein adds selective advantages to the microorganism.
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  • Resultat 1-8 av 8

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