2. 0.1 mL of a protein solution of concentration of 7 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 3 mL of this solution was then mixed with 27 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
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- Protein Solubility 3.5 5.5 5 5 0.068 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.130 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 15 PH 7.5 1.5 4.5 5 0.027 3 0.042 Protein Solubility Versus pH 6.5 6 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 7.5 7.5 50 0.032 0.053 8.5 50 0.054 0.100 21.429% 9 Please provide a brief discussion and explanation of the results. (using isoelectric point and net charge to explain)3. 4. A protein solution is prepared by dissolving 800 µg of protein in 200 µL of water. A 150 μL sample of this solution is diluted to a total volume of 4.5 mL. How many mg of protein will be in a 3 mL sample of the diluted protein solution? Space to show your workings:Calculate the unknown concentration of the PROTEIN C with an absorbance value of A412 given the standard curve indicated in the table below. Write your final answer (NUMBER ONLY) in two decimal places rounded off. Protein concentration (µg/mL) 0 0.02 0.04 0.06 0.08 0.10 Your answer APIENT Absorbance 0.000 0.161 0.284 0.438 0.572 0.762
- The calibration curve shown below was used to analyze an unknown protein solution. What is the concentration of the unknown solution, if the absorbance of the unknown is 0.505? Answer in ug/mL. 1.2 y%3D0.005x+0.061 R=0.992 0.8 0.6 0.4 0.2 50 100 150 200 250 Concentration ug/ml AbsorbanceMolar concentration 1.0 Molar concentration Depicted below is a cell membrane separating two closed compartments, each filled with one liter of H₂. You add one mole of each of the molecules as shown below. The molecule to which the membrane is most permeable diffuses across at a net rate of 0.5 moles/hour. Based on this information, answer the following questions. 1.0 0₂ Nat 0.5- fructose glycerol K+ 2. Graph the expected relative concentrations of each solute in the right hand compartment as a function of time. 1 Time in hours Nat 1. Immediately after adding these solutes, will there be a net movement of H₂O molecules across the membrane in one direction? If so, in which direction and why? through right K+ 3. Finally, you add ATP to the left side compartment at the time indicated by the arrow below, and measure concentration of Nat and K+ in the right side compartment. Your results are graphed below. Propose a hypothesis to explain the results you obtained in this experiment. 2 (10…Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…
- at 257 nm) is dissolved in 2.5 mL of buffer. A 250 microliter aliquot is removed and placed in a 1.0 cm A sample of adenosine triphosphate (ATP) (MW 507, ɛ = 14,700 M'cm cuvette with sufficient buffer to give a total volume of 2.0 mL. The absorbance of the sample at 257 nm is 2.0. Calculate the weight of ATP in the original 2.5 mL sample. (Choose the correct value from the drop-down list provided. The values of weight are listed in units of milligrams.) Weight of ATP: v mgGiven a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.The following stock solutions are available to make a protein extraction buffer: 100% Nonidet P-40, 1 M Tris-Cl, and 0.5 M EDTA. What quantity of the original stocks will be needed to make 250 ml of buffer with the following final concentrations: 0.5% Nonidet, 150 mM Tris-Cl, and 10 mM EDTA?
- Protein Solubility 3.5 5 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 pH 15 7.5 1.5 4.5 5 0.027 3 0.042 5.5 5 0.068 0.130 Protein Solubility Versus pH 6 6.5 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 Please provide a brief discussion and explanation of the results. 7.5 7.5 50 0.032 0.053 9 8.5 50 0.054 0.100 21.429%Size Size Crude Anion Cation 2) Exclusion Exclusion Lysate Exchange Exchange 1 2 Total Protein Concentration 15.2 6.6 2 3.75 4.7 (mg/mL) Final Sample Volume 60 30 20 4 3 (mL) Enzyme Specific Activity 0.43 1.7 7.25 18.3 12.5 (units/mgprotein) Based on your protein purification sample data, in which of the purification steps in your protocol did you effectively purify your enzyme? Select all that apply. a) anion exchange correct b) cation exchange correct c) size exclusion 1 correct d) size exclusion 2In a 0.1000 M acetic acid solution at 25 degrees celsius , the acid ionizes to the extent of about 1.34 %. Since each molecule of acetic acid which ionizes produces 1 H+ ion and 1 C2H3O2- ion, the concentration in the solution are: HC2H3O2 < -----------> H+ + C2H3O2-