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- 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?Which of the following statements are true about stacking and separating gels? a. The holes is the separating gel are much smaller than the ones in the stacking gel. b. The stacking gel is at a pH of 6.9, while separating gel is at a pH of 8.9 c. The higher pH in separating gel causes the glycine buffer to accelerate more and thus leaving behind the proteins to stack at the interface. d. The smaller holes in separating gel slows down the mobility of the proteins at the interface.We have isolated a mixture of 2 protein of the same molecular weight but different isoelectric points. The isoelectric points are 7.5 for Protein A and 9.0 for Protein B. What would be the order of elution from a cation exchange column if a buffer of pH 7 is used? Group of answer choices Both proteins will remain in the column. Both proteins will elute simultaneously Protein B followed by Protein A Protein A followed by Protein B
- One tenth mL of a protein solution was diluted with 2.5 mL of water. The A280 of the diluted solution was 0.25. How many mL of the original protein solution and water should be mixed to make 1.0 mL of solution of A280 = 0.80?If several like-charged proteins are bound simultaneously to an ion exchange column, they can be separated by gradually increasing the salt concentration (applying a “gradient”). A CM-Sepharose column has three proteins bound to it: A (pI = 7.9), B (pI = 7.4), and C (pI = 8.7). At pH = 7.0, the salt concentration on the column is gradually raised from 0 to 500 mM. In what order will the proteins elute? Explain.A protein has a pI point which can be used to separate proteins using ion exchange. If you have an anion exchange column and access to buffers of any pH, how could you isolate a protein with a pI of 7 from a mixture of proteins which also has proteins with pI points of 3 and 5.
- Which of the following about protein denaturation is not trueA. It is always irreversible B. It is a shape change C. It may be due to pH / temperature change D. Most of the proteins denature when transferred from aqueous environment to organs solvents E. Its function is lost.You had a second solution with an unknown concentration of Protein X that had to be diluted 4x before you could measure the absorbance. The diluted solution had an absorbance of 0.76. What is the concentration of the diluted solution in ug/ml and what is the concentration of the original solutionDescribe how you would prepare 500mL Edward’s buffer when you have 1M Tris-CL (pH 7.5), 1M NaCl, 50mM EDTA, and 10% SDS in the lab. the final concentration in Edward’s buffer: 200mM Tris-Cl, pH 7.5: lysis buffer, regulates pH and osmolality 250mM NaCl: removes protein bound to DNA 25mM EDTA (Ethylenediaminetetraacetic acid): Chelating agent that depletes metal ions 0.5% SDS (sodium dodecyl sulfate): surfactant commonly found in cleaning products. In this lab it is used to lyse cells.
- A 20µL unknown protein was mixed with 80µL of water. Then, 10µL of this mixture was added with 10µL Bradford reagent and diluted with water to a total volume of 100µL. The absorbance at 595 nm shows 0.08 units. Solve for the protein concentration (in mg/mL) of the original unknown protein. How much protein (in mg) is in the 20uL sample? Express your answer in 3 significant figures.Which factors will cause protein denaturation? Group of answer choices a. aqueous phosphate buffer b. heavy metals - Hg2+, Pb2+, Ag+ c. small metal ions - Na+, Ca2+, Cl- d. changes in pH e. use of detergents or soaps f. Tris a buffer commonly used with proteinsCalculate 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