12 research outputs found

    Performance data for Sedum album plants in a paired-plant experiment

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    The present file contains data on vegetative and reproductive performance traits (shoot and panicle number) measured on Sedum album plants, paired with a genetically different or identical individual in a 4-year garden experiment. The paired individuals in two-genotype trays differed in anthocyanin pigmentation (green vs. red) to allow separation of plants during data collection. The data were used to estimate direct and indirect genetic effects on plant performance

    Means, 95 percent confidence intervals (CI) and within-pair correlations (<i>r</i>) for traits measured on <i>S. album</i> plants used in the present experiment.

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    <p><i>Note</i>: Analyses based on ln-transformed data. * <i>P</i><0.05, ** <i>P</i><0.01, *** <i>P</i><0.001.</p>a<p>Back-transformed values (<i>n</i> = 400).</p>b<p>Product-moment correlations (<i>n</i> = 160).</p><p>Means, 95 percent confidence intervals (CI) and within-pair correlations (<i>r</i>) for traits measured on <i>S. album</i> plants used in the present experiment.</p

    <i>Sedum album</i> growing on a moss cushion in an alvar area on Öland, SE Sweden.

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    <p>Photo taken in the autumn of 2013.</p

    The direct mean of each genotype compared with the indirect mean induced by the same genotype on a neighbouring individual of another genotype.

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    <p><i>Note</i>: Entries are back-transformed least-square means from ANOVAs on ln-transformed data.</p>a<p>Codes refer to different genotypes of the red (R) and green (G) colour morph.</p><p>The direct mean of each genotype compared with the indirect mean induced by the same genotype on a neighbouring individual of another genotype.</p

    Results from ANOVAs (<i>F</i>-ratios) and variance component analyses for traits measured on <i>S. album</i> plants paired with a genetically identical individual.

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    <p><i>Note</i>: Analyses based on ln-transformed data. * <i>P</i><0.05, ** <i>P</i><0.01, *** <i>P</i><0.001.</p>a<p>Degrees of freedom  = 1, 6.</p>b<p>Degrees of freedom  = 6, 72.</p>c<p>Percentage of variance attributable to genotype.</p><p>Results from ANOVAs (<i>F</i>-ratios) and variance component analyses for traits measured on <i>S. album</i> plants paired with a genetically identical individual.</p

    The relationship between direct and indirect genetic effects for panicle number in 2008.

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    <p>The scatter plot compares the direct mean of each genotype (averaged across pair mates) with the indirect mean induced by that genotype on its neighbour (averaged across pair mates). Pearson <i>r</i> = −0.89, <i>P</i><0.01.</p

    Results from ANOVAs (<i>F</i>-ratios) and variance component analyses for traits measured on <i>S. album</i> plants paired with a genetically different individual.

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    <p><i>Note</i>: Analyses based on ln-transformed data. * <i>P</i><0.05, ** <i>P</i><0.01, *** <i>P</i><0.001.</p>a<p>Degrees of freedom  = 1, 6–11.</p>b<p>Degrees of freedom  = 6, 18.</p>c<p>Degrees of freedom  = 18, 128.</p>d<p>Percentage of variance attributable to different genotype effects.</p><p>Results from ANOVAs (<i>F</i>-ratios) and variance component analyses for traits measured on <i>S. album</i> plants paired with a genetically different individual.</p

    Homology-modelled <i>M</i>. <i>cinxia</i> Pgi structures showing the structural variation at AA sites 111 & 372.

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    <p>A) Pgi dimer with one monomer shown in yellow and the other shown in green. The two Pgi AA sites (111 and 372) of interest are shown in purple and a competitive inhibitor (5-phosphoarabinonate, in red) of the enzyme substrate indicates the locations of the catalytic centres. B) shows the AA residues that are within the 10Å distance of the AA site 111, which is located on a surface loop. At site 111, comparing to the neutral residue Gln111 (in yellow) of Pgi-f, the alternative basic residue Lys111 (in purple) of Pgi-non-f “pushes” the nearby basic residue Arg at site 113 (yellow when site 111 has Gln while purple when site 111 has Lys) away. Moreover, a hydrogen bond is formed between the Gln111 carbonyl oxygen atom and the side chain guanidino group of Arg113, while no hydrogen bond is found between Lys111 and Arg113. C) and D) show the AA residues within the 10Å distance of either His372 (in purple) of Pgi-f or Asp372 of Pgi-non-f (in purple). Site 372 is close to an inter-monomer interaction between Glu373 (in yellow) that is located in the same monomer (in yellow) as site 372 and residue Lys472 (in green) that is located in the other monomer (in green). Compared to the basic His372 of Pgi-f, the acidic Asp372 of Pgi-non-f “pushes” the acidic Glu373 closer to Lys472: the distances between GLu373 and Lys472 is 4.94 Å and 7.03 Å, respectively, when Asp372 and His372 occur. In addition, a hydrogen bond between the side chain carboxyl group of the Glu373 and the imidazole ring of His372 draws Glu373 away from the inter-monomer interface, while only the backbone amino group of Glu373 forms a hydrogen bond to the side chain carboxyl group of Asp372.</p

    ONIOM(QM:AMOEBA09) Study on Binding Energies and Binding Preference of OH, HCO, and CH<sub>3</sub> Radicals on Hexagonal Water Ice (I<sub>h</sub>)

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    We have combined the AMOEBA09 polarizable force field with the ONIOM­(QM:MM) method to rationalize binding energies and binding preferences of the OH, HCO, and CH<sub>3</sub> radicals on crystalline water ice (I<sub>h</sub>). ONIOM­(M062X:AMOEBA09) and ONIOM­(wB97XD:AMOEBA) calculations suggest that the dangling hydrogen (<i>d</i>-H) or dangling oxygen (<i>d</i>-O) on the binding sites play an important role on the binding energies. Depending on the dangling nature at the binding site, a range of binding energies is found for the OH radical (0.67–0.20 eV), HCO radical (0.42–0.12 eV), and CH<sub>3</sub> radical (0.26–0.11 eV). The binding energies of these radicals are larger in the presence of both <i>d</i>-H and <i>d</i>-O at the binding site. On the other hand, binding energies are weaker in the presence of only <i>d</i>-H or <i>d</i>-O at the binding site. The ONIOM­(QM:AMOEBA09) methodology is found to be a useful approach to calculate binding energies of atoms, radicals, and molecules on I<sub>h</sub>
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