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:
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- 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:To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?Given a stock protein solution with a concentration of 3 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
- 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…How will you make a series of two-fold dilutions of a protein solution to give 5 different concentrations? The initial concentration of the protein solution is 70ng/μl and the final volume needed (for an experiment) is 10 µl for each dilution.A researcher prepares 100 mL of aqueous solution containing 0.1 g of a protein. The researcher then uses an experimental apparatus ,where he notes that, at room temperature (300K) and atmospheric pressure (101.325 kPa), distilled water flows naturally into the solution compartment. However, when he applies an extra pressure of 1000 Pa he observes that the flow of distilled water ceases and the system is in balance. Calculate the molar mass of this protein, in kDa (1 Da = 1 g/ mol); Why does the flow of distilled water cease with the application of the pressure of 1000 Pa? Explain in terms of potential chemicals. %3D
- A large chaperone protein complex GroEL is approximately 16 nm in diameter. When it is dissolved in water at 300 K, estimate the average time it will take for GroEL to diffuse a distance of 500 nm (0.5 micron). The viscosity of water is 10-3 Pa*s.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)Molar 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…
- if you had a protein sample solution of unknown concentration which gave an absorbance of 0.992 after the two-fold dilution (25 μL water + 25 μL sample). If the standard curve we constructed. what would you need to do to your sample in order to find its protein concentration more accurately?A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…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?