3,449 research outputs found

    Aeration and its Effects on Zooplankton

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    The purpose of this study was to examine the effect of aeration primarily on zooplankton

    Acoustic scattering by impedance screens/cracks with fractal boundary: well-posedness analysis and boundary element approximation

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    We study time-harmonic scattering in Rn\mathbb{R}^n (n=2,3n=2,3) by a planar screen (a "crack" in the context of linear elasticity), assumed to be a non-empty bounded relatively open subset Γ\Gamma of the hyperplane Rn−1×{0}\mathbb{R}^{n-1}\times \{0\}, on which impedance (Robin) boundary conditions are imposed. In contrast to previous studies, Γ\Gamma can have arbitrarily rough (possibly fractal) boundary. To obtain well-posedness for such Γ\Gamma we show how the standard impedance boundary value problem and its associated system of boundary integral equations must be supplemented with additional solution regularity conditions, which hold automatically when ∂Γ\partial\Gamma is smooth. We show that the associated system of boundary integral operators is compactly perturbed coercive in an appropriate function space setting, strengthening previous results. This permits the use of Mosco convergence to prove convergence of boundary element approximations on smoother "prefractal" screens to the limiting solution on a fractal screen. We present accompanying numerical results, validating our theoretical convergence results, for three-dimensional scattering by a Koch snowflake and a square snowflake

    Acetylation of importin-α nuclear import factors by CBP/p300.

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    Histone acetylases were originally identified because of their ability to acetylate histone substrates 1, 2 and 3. Acetylases can also target other proteins such as transcription factors 4, 5, 6 and 7. We asked whether the acetylase CREB-binding protein (CBP) could acetylate proteins not directly involved in transcription. A large panel of proteins, involved in a variety of cellular processes, were tested as substrates for recombinant CBP. This screen identified two proteins involved in nuclear import, Rch1 (human importin-α) and importin-α7, as targets for CBP. The acetylation site within Rch1 was mapped to a single residue, Lys22. By comparing the context of Lys22 with the sequences of other known substrates of CBP and the closely related acetylase p300, we identified G/SK (in the single-letter amino acid code) as a consensus acetylation motif. Mutagenesis of the glycine, as well as the lysine, severely impaired Rch1 acetylation, supporting the view that GK is part of a recognition motif for acetylation by CBP/p300. Using an antibody raised against an acetylated Rch1 peptide, we show that Rch1 was acetylated at Lys22 in vivo and that CBP or p300 could mediate this reaction. Lys22 lies within the binding site for a second nuclear import factor, importin-β. Acetylation of Lys22 promoted interaction with importin-β in vitro. Collectively, these results demonstrate that acetylation is not unique to proteins involved in transcription. Acetylation may regulate a variety of biological processes, including nuclear import
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