993 research outputs found
Albrecht Fitness Studio Business Plan
No full textThis business outlines what it would take to develop a designer fitness studio in Charlotte, NC. The plan contains all key aspects of a business plan, from an executive summary to a cash flow statement. The author is also the acting CEO of the company Albrecht Fitness and plans to follow through with the plan in the next 5 years. This business plan proposes an $80,000 loan needed from potential investors. The components of this business plan outline the company's potential profitability, key strategies, and overall business model
PISM glacial cycle sensitivity experiments of the Antarctic Ice Sheet
No full textThis dataset contains PISM simulation results (http://www.pism-docs.org) of the Antarctic Ice Sheet based on code release v1.0-paleo-ensemble (https://doi.org/10.5281/zenodo.3574033). PISM is the open-source Parallel Ice Sheet Model developed mainly at UAF, USA and PIK, Germany.
With the help of added python scripts, all figures can be reproduced as in the journal publication:
- Albrecht et al., 2020, doi:10.5194/tc-14-599-2020.
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Data:
Find PISM results as netCDF data. See 'README.md' for a list of all performed experiment.
All forcing input data for the experiments and plots can be downloaded and remapped via https://github.com/pism/pism-ais. Some of the original input data files are freely available, for others please contact the author or the corresponding data publisher.
Figure plotting scripts (jupyter notebook based on python, see https://jupyter.org) in 'plot_scripts' access the uploaded PISM results in 'model_data' and save the plots to 'final_figures'. Jupyter notebook can be run in the browser and shared, see https://nbviewer.jupyter.org/url/www.pik-potsdam.de/~albrecht/notebooks/paleo_paper/paleo_paper_final.ipynb.
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Contact:
Albrecht, Torsten ([email protected]) ; Potsdam-Institute for Climate Impact Research (PIK), Potsdam, German
pism/pik/paleo_07dev: PISM version as used in Kingslake, Scherer, Albrecht et al. Nature publication
No full text<p>This is a code release of the Parallel Ice Sheet Model (PISM) used for paleo simulations of the Antarctic Ice Sheet as discussed in</p>
<p><a href="https://doi.org/10.1038/s41586-018-0208-x">Kingslake, J., Scherer, R.P., Albrecht, T., Coenen, J., Powell, R.D., Reese, R., Stansell, N.D., Tulaczyk, S., Wearing, M.G. and Whitehouse, P.L., 2018. Extensive retreat and re-advance of the West Antarctic Ice Sheet during the Holocene. <em>Nature</em>, <em>558</em>(7710), p.430</a>.</p>
<p>For input data and plotting scripts please contact the author ([email protected]).</p>
Crystal structure of pyrogallol phloroglucinoltranshydroxylase, an Mo enzyme capable ofintermolecular hydroxyl transfer between phenols
No full textThe Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalousdiffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalousdiffraction technique. Tranhydroxylase is a heterodimer, with the active Mo molybdopterin guanine dinucleotide (MGD)2 site in the α-subunit, and three [4FeO4S] centers in the β-subunit. The latter subunit carries a seven-stranded, mainly antiparallel β-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.publishe
Una nota su Albrecht Dürer e Vitruvio = A Note on Albrecht Dürer and Vitruvius
No full textIn questo saggio l’autore propone una riconsiderazione globale del rapporto di Albrecht Dürer con il De Architectura di Vitruvio, prestando costante attenzione alle fonti rimaste. Inoltre, l’autore indaga anche un aspetto trascurato di questo rapporto, che riguarda la significativa accoglienza dei trattati di Dürer tra i traduttori e i commentatori di Vitruvio tra il XVI e il XVII secolo.AbstractIn this essay the author proposes an overall reconsideration of Albrecht Dürer’s relationship with Vitruvius’ De Architectura, paying constant attention to the surviving sources. Furthermore, the author also investigates an overlooked aspect of this relationship that concerns the significant reception of Dürer’s treatises among Vitruvius’ translators and commentators between the XVIth and the XVIIth centuries
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase
No full textThe tungsten iron sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 Å now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.publishe
Binding and Reduction of Sulfite by Cytochrome c Nitrite Reductase
No full textPentaheme cytochrome c nitrite reductase (ccNiR) catalyzes the six-electron reduction of nitrite to ammonia as the final step in the dissimilatory pathway of nitrate ammonification. It has also been shown to reduce sulfite to sulfide, thus forming the only known link between the biogeochemical cycles of nitrogen and of sulfur. We have found the sulfite reductase activity of ccNiR from Wolinella succinogenes to be significantly smaller than its nitrite reductase activity but still several times higher than the one described for dissimilatory, siroheme-containing sulfite reductases. To compare the sulfite reductase activity of ccNiR with our previous data on nitrite reduction, we determined the binding mode of sulfite to the catalytic heme center of ccNiR from W. succinogenes at a resolution of 1.7 A. Sulfite and nitrite both provide a pair of electrons to form the coordinative bond to the Fe(III) active site of the enzyme, and the oxygen atoms of sulfite are found to interact with the three active site protein residues conserved within the enzyme family. Furthermore, we have characterized the active site variant Y218F of ccNiR that exhibited an almost complete loss of nitrite reductase activity, while sulfite reduction remained unaffected. These data provide a first direct insight into the role of the first sphere of protein ligands at the active site in ccNiR catalysis
Una nota su Albrecht Dürer e Vitruvio
No full textIn this essay the author proposes an overall reconsideration of Albrecht Dürer’s relationship with Vitruvius’ De Architectura, paying constant attention to the surviving sources. Furthermore, the author also investigates an overlooked aspect of this relationship that concerns the significant reception of Dürer’s treatises among Vitruvius’ translators and commentators between the XVIth and the XVIIth centuries. In questo saggio l'autore propone una riconsiderazione globale del rapporto di Albrecht Dürer con il De Architectura di Vitruvio, prestando costante attenzione alle fonti rimaste. Inoltre, l'autore indaga anche un aspetto trascurato di questo rapporto, che riguarda la significativa accoglienza dei trattati di Dürer tra i traduttori e i commentatori di Vitruvio tra il XVI e il XVII secolo
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