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- 2 a. You are trying to purify protein C from a mixture of proteins noted in the above Table. If you had only one type of column to choose from, which one would allow you to purify protein C with the least number of contaminants? Size exclusion column Ion exchange column Affinity chromatography using glucose as the bait Affinity chromatography using NAD as the bait Please explain why you chose the column above based upon the properties of the column AND the proteins in the Table.6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.1. In Gel filtration chromatography, when will you stop collecting eluents if sample is not colored? 2. How does SDS-PAGE separate proteins and peptides from each other? Explain. 3. Explain the Donnan Membrane Phenomenon. Why is it important for the homeostasis of the cell?
- Bradford technique makes use of the Coomassie blue dye that binds to the protein, with the complex absorbing strongly at 465 nm. O True O FalseConsider the following properties of the protein components of a sample mixture as provided in the table below. Protein Molecular IpH Percentage of polar amino acid residues Weight (kDa) (%) АСЕ 200 7 20 CLU 25 65 DIA 100 10 40 НЕА 50 801. You want to purify a protein using anion exchange column chromatography. In this technique, the solid state beads are positively charged. What charge would you want your protein to have in order for it to "stick" to the beads? Neutral Positive Negative 2. In your anion exchange experiment, your protein of interest has a pI of 6.0. Which of the following buffer solutions would you want to use when loading your protein extract onto the column so that your protein "sticks" to the beads? pH 4.5 pH 7.3 pH 6.0 3. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer consisting of 2 alpha subunits, 1 beta subunit, and 2 gamma subunits, how many bands would you expect to see on your gel? The alpha subunits are 32kDa. The beta subunit is 32kDa. The gamma subunits are 15kDa. 1 5 2 3 4. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer…
- A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.VITATI KEY: Positive charge: Purple, Negative Charge: Pink Hydrophilic: Green Hydrophobic: Brown MOSTU. TOUT um b. Now change the second pull down to oil. What changes? וועען a. Set the first pull down to show charge and hydrophobicity and the second pull down as water. Click generate random protein, and then select random mix (last option). Run the simulation (arrow in center of playbar). What do you notice? (ie What type of amino acid are on the outside?) When you run it again, what is the same and what is different? c. Now change the second pull down to vacuum. What changes? What type of interactions remain? d. Now instead of ‘random mix’, click Mostly hydrophobic and toggle between oil and water. What do you notice? e. Lastly click All hydrophilic and toggle between oil and water. What do you notice? 2. What are the monomers (one subunit) of a polypeptide called? ● On the left half of the space below, draw a simple structure of a protein monomer with uncharged functional groups and…A solution containing two globular proteins each with a single subunit (one is "large" with a radius of 47 Å and the other is "small" with a radius of 16 A) is applied to a gel-filtration (i.e. size-exclusion) column. What is the most likely outcome? O a The outcome will depend on which protein has the most negative surface charge. O b. The small protein elutes before the large protein. O C. The large protein elutes before the small protein. O d. Both proteins elute together. O e. The outcome will depend on the pH of the solution.
- 14. A protein mixture consisting of proteins A, B, and C was subjected to various protein purification steps. First, the protein mixture was applied to an anion ion exchange column. When the column was washed with an increasing concentration gradient of chloride ions, the order of elution of the three proteins was B, then C, and finally A. Next, the protein mixture was chromatographed on a gel filtration column. The order of elution of the three proteins from this column was C, A, B. Finally, the protein mixture was passed over a chromatography column containing a Ni-NTA affinity matrix. Only protein A was retained by the column. Answer the following (i) Which protein (A, B, or C) has the highest and lowest positive charge (ii) Which protein has the highest and lowest mass (ii) Which protein has an affinity for the Ni-NTA matrix and whyYou perform electrophoresis of 3 proteins, Hemoglobin (pl: 6.8), DNA Polymerase (pl: 5.2) and Porcine pepsin (pl: 1.0) in a Tris-Glycine buffer (pH 5.2). (pl = Isoelectric point). Select which of the following is true. O All proteins will migrate at the same rate O All proteins will migrate at the same direction Porcine pepsin will migrate toward the electrode Porcine pepsin will not migrate and stay in the wellA certain heterotetrameric protein was run in PAGE under different reducing and denaturing conditions. The resulting block diagram is shown below:How many bands, and at what MWs, would appear in a separate SDS-PAGE run, with dithiothreitol + HCl included in the loading buffer?A. 2 : 150, 200 kDaB. 2 : 100, 250 kDaC. 3 : 50, 100, 150 kDaD. 4 : 50, 100, 150, 350 kDa