Julie is explaining to her employee, Richard, the parameters…
Questions
Julie is explаining tо her emplоyee, Richаrd, the pаrameters оf his next project (scope, length, content, deliverables, etc.). In such situations, I indicated that he should…
Pаrt C: Life Cycle Assessment - Mаtrix Fоrmulаtiоn [45 pоints] Using the linear algebra LCA framework from the lecture and mean parameter values, quantify the CO2 and water impact per battery for both the brine and hard-rock pathways. Use the following hints: Construct the functional demand vector. Construct two unit process matrices: p1 for lithium carbonate production and p2 for energy production. Order the rows in the unit process matrices as follows: lithium carbonate [kg per battery], energy [MJ per battery], carbon dioxide [kg CO2 per battery], and water [m3 per battery]. Construct the A and B matrices and determine the scaling matrix Determine the g matrix Part D: Sensitivity Analysis D1. Using the Python notebooks provided in the lectures, conduct a Sobol Analysis to determine the most influential variables for both CO2 and water impact. [10 points] D2. Using the Python notebooks provided in the lectures, conduct a Moment Independent Sensitivity Analysis (MISA) to determine the most influential variables for both CO2 and water impact. [10 points] D3. In the Sobol indices results, is the most dominant input parameter driving CO2 and water impacts for the brine pathway different? [5 points] D4. In the Sobol indices results, is the most dominant input parameter driving CO2 and water impacts for the hard rock pathway different? [5 points] D5. In the MISA indices results, is the most dominant input parameter driving the CO2 impact across the brine and hard rock pathways different? [5 points] D6. In the MISA indices results, is the dominant input parameter driving water impact across the brine and hard rock pathways different? [5 points] D7. Is there a difference between the Sobol and MISA analysis? [5 points]
This infоrmаtiоn is fоr questions 15–22. The following is from а published (Sept. 2014) purificаtion scheme for the isolation of a toxic protein from the venom of the blunt-nosed viper, a snake native to North Africa. Answer the following questions about the techniques used to purify and characterize the protein. Text from the reference cited below: “2.2. Purification of lebecinAbout 300 mg of crude venom of M. lebetina was dissolved in a small volume of 0.2 M ammonium acetate, pH6.8, applied to a column packed with Sephadex G-75 equilibrated with the same buffer (Pharmacia, Uppsala, Sweden) and eluted as previously described ( Sarray et al., 2003). The fraction II, containing anti-adhesive activity, was pooled and lyophilized for further purification. It was applied on a Mono S (HR5/5) column previously equilibrated with 50 mM HEPES/HCl pH 7.5 and eluted with linear NaCl gradient (0-1 M) at a flow rate of 1 ml/min. Finally, the fractions obtained were purified on C8 column (250 x 4.6 mm, 5 mm; Beckman) by reversed phase HPLC equilibrated in 0.1% trifluoroacetic acid (TFa) in 10% acetonitrile and elution was achieved using a linear acetonitrile gradient (10-80%) at a flow rate of 1 ml/min. Proteins concentration of purified lebecin was quantified according to the protocol provided by the BCA kit (Pierce Chemical Co.) using bovine serum albumin (BSA) as a standard. The homogeneity and the apparent molecular mass of the purified lebecin and its subunits were determined by SDS_PAGE method using 12.5% polyacrylamide gel with or without reduction by 2% beta-mercapto-ethanol. Proteins were stained with Coomassie brilliant blue R-250 (Sigma). Purified lebecin was reduced and alkylated as described previously by Sarray et al. (2003). The S-alkylated proteins chains were then desalted and separated by reverse phase HPLC on a C8 column as described above for protein purification. 2.3. N-terminal amino acid sequence determinationThe N-terminal amino acid sequences of lebecin subunits were determined by automated Edman degradation using a PROCESE instrument from Applied Biosystem (Foster city, CA). Sequence homology was evaluated by a computer search in the protein sequence database (BLAST search).” Jebali, J., Fakhfekh, E., Morgen, M., Srairi-Abid, N., Majdoub, H., Gargouri, A., El Ayeb, M., Luis, J., Marrakchi, N., & Sarray, S. (2014). Lebecin, a new C-type lectin like protein from Macrovipera lebetina venom with anti-tumor activity against the breast cancer cell line MDA-MB231. Toxicon : official journal of the International Society on Toxinology, 86, 16–27.