Se alquila 'alejamiento' turístico sobre cementerio indio

La noticia aparecía hace unos meses en losmedios: en el barrio de Poble Sec (Barcelona) estaban construyendo un edificio con seis apartamentos plurifamiliares de madera dirigidos a un mercado de turismo responsable. La promotora de estos apartamentos explicaba que se oponía al "turismo de borrachera" y a la "masificación de los barrios" y que apostaba por otros valores como son la "ecología" y lo "social". Todo un manifiesto[...] La notícia apareixia fa uns mesos en losmedios: al barri de Poble Sec (Barcelona) estaven construint un edifici amb sis apartaments plurifamiliars de fusta dirigits a un mercat de turisme responsable. La promotora d'aquests apartaments explicava que s'oposava al 'turisme de borratxera' i de la 'massificació dels barris' i que apostava per altres valors com són la 'ecologia' i el 'social'. Tot un manifest[...

Additional file 2: of Reference-guided de novo assembly approach improves genome reconstruction for related species

Table of evaluation statistics at low coverage. (XLSX 51 kb

Additional file 1 of Positional bias in variant calls against draft reference assemblies

Supplementary figures. (PDF 1499 kb

Additional file 7 of Development of a prediction system for tail-anchored proteins

Table S4. Initial conditions for the MP model. (PDF 37 kb

MD simulations of Isd•heme•Isd ternary complexes.

<p>(A and D) Overall structures of the docked complexes IsdH-N3, IsdA-N, IsdC-N, and heme are represented in cyan, yellow, orange, and purple, respectively. The IsdH-N3•heme•IsdA-N and IsdA-N•heme•IsdC-N snapshots were obtained in MD simulations at 1,000 and 900 ns, respectively. (B and E) Plots of distances in MD trajectories; black, green, red, and blue traces represent distances between side-chain Oγ atoms of conserved serine residues and proximal carboxyl groups of heme, between Oη atoms of the primary tyrosine residues and iron, and between the secondary tyrosine and iron, respectively. (C and F) Plots of RMSD values; crystal structures were used as reference structures. Panel F: RMSD values that were calculated excluding the β7-β8 hairpin in IsdC-N (residues Asp-118 to Tyr-136) are presented in the blue trace.</p

MD simulations of Isd•heme•Isd ternary complexes.

<p>(A and D) Overall structures of the docked complexes IsdH-N3, IsdA-N, IsdC-N, and heme are represented in cyan, yellow, orange, and purple, respectively. The IsdH-N3•heme•IsdA-N and IsdA-N•heme•IsdC-N snapshots were obtained in MD simulations at 1,000 and 900 ns, respectively. (B and E) Plots of distances in MD trajectories; black, green, red, and blue traces represent distances between side-chain Oγ atoms of conserved serine residues and proximal carboxyl groups of heme, between Oη atoms of the primary tyrosine residues and iron, and between the secondary tyrosine and iron, respectively. (C and F) Plots of RMSD values; crystal structures were used as reference structures. Panel F: RMSD values that were calculated excluding the β7-β8 hairpin in IsdC-N (residues Asp-118 to Tyr-136) are presented in the blue trace.</p

Proposed heme transfer mechanism from IsdH-N3 to IsdC via IsdA.

<p>The sides of heme are shown in black and white. Heme is inverted upon formation of the complex between acceptor and donor NEAT domains.</p

Two-dimensional potential energy surface of the system of two phenols and an Fe(III)-porphine.

<p>Black contour lines are at intervals of 3 kcal/mol.</p

Optimization of structures using the ONIOM method.

<p>Residues of IsdH-N3, IsdA-N, and IsdC-N are shown in cyan, yellow, and orange, respectively. Heme is shown in purple. (<b>A</b>) IsdH–Tyr642 and IsdA–Tyr170 are deprotonated in the IsdH-N3•heme•IsdA-N complex and (<b>B</b>) IsdA–Tyr166 and IsdC–Tyr132 are deprotonated in the IsdA-N•heme•IsdC-N complex.</p

Additional file 9: of Silhouette Scores for Arbitrary Defined Groups in Gene Expression Data and Insights into Differential Expression Results

Examples of AS estimates for two- and three-group data. The procedures for analyzing Nakai’s MAS-quantified data consisting of 31,099 probesets × 24 samples are provided. Example 1 compares three-group data with four BRs, 4 BAT_fed samples vs. 4 WAT_fed samples vs. 4 LIV_fed samples, with AS = 0.460. Example 2 compares three-group data with two BRs, “BAT_fed1 and 2” vs. “WAT_fed1 and 2” vs. “LIV_fed1 and 2,” with AS = 0.438. Example 3 compares three-group data with two BRs, “BAT_fed1 and BAT_fas1” vs. “BAT_fed2 and BAT_fas2” vs. “BAT_fed3 and BAT_fas3,” with AS = − 0.185. Example 4 compares two-group data with four BRs, 4 BAT_fed samples vs. 4 WAT_fed samples, with AS = 0.374. Example 5 compares two-group data with four BRs, 4 BAT_fed samples vs. 4 LIV_fed samples, with AS = 0.657. (R 3 kb