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- 5. What will happen to a protein if subjected to high tempuraturea?1. Why must the solution to be tested with ninhydrin be neutral? 2. Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?5 You need to separate the following three proteins, Protein A (MW 76 600 Da; pI 4.5); Protein B (MW 70 000 Da and pI 8.2) and Protein C (MW 42 000; pI 8.6). Describe what column/s you would use, the pH of the buffer/s you would use, which proteins are retained on the column and how you would elute the bound protein/s. How would you monitor where the protein peaks elute and whether the protein in each peak is pure of not?
- 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.1. How do you prepare 25 mL of a 0.4X solution of SDS from a 20X stock?2. How do you prepare 50 mL of a 0.25X solution of Trisethylenediaminetetraacetic acid (TE) buffer from a 100X stock?Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073x
- If I had a standard with 2.0 mL of Bradford reagent then added 50μL of 250 μL/mL ; what would be the concentration of original protein?6. The Worthington's manual reports two extinction coefficients for lysozyme. Corvert one into the other. What is the absorbance at 280 nm of a 0.1 mg/mL lysozyme solution? Use both coefficients to estimate the resultF. How much of a 100 mg/mL stock of Ampicillin would you need to add to 400 mL for a 100 ug/mL final concentration? What fold stock is this?
- 1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.What is the basis for the separation of proteins by the following techniques? (a) gel-filtration chromatography (b) affinity chromatography (c) ion-exchange chromatography (d) reverse phase HPLCThe protein concentration of a known standard is 100mg/mL If you prepared a serial dilution, mixing 10μL of protein with 40μL of water what would be concentrations of the first 3 dilutions?