You perform a Bradford assay. You obtain the absorbance values listed below from the BSA samples; your protein sample yields an absorbance of 1.3; what is the protein concentration of your sample? How did you determine that?
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- protein is purified and at a concentration of 600 μg in 1.75 ml of buffer. You do an assay with your purified protein, and the assay requires 25 μg of biochemisfunase. What volume of the purified biochemisfunase would yield 25 μg? Show your calculation.When you graph your protein assay data in Excel, should you include the absorbance of your unknown BSA sample? Explain why or why notThe A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
- Using Bradford Assay, plot the standard curve and find the unknowns. Protein Concentration A595 of sample 0 0 3 0.220 6.5 0.383 12 0.667 18.8 0.930 24.2 1.090 Unknown 1 1.085 Unknown 2 0.708 Unknown 3 0.193To 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?A 1/10 dilution of enzyme extract has been done for the protein assay. The experimental results are given below. Tube Phosphate buffer 0.1 M pH 7 (µL) Diluted enzyme extract (uL) Bradford reagent (mL) DO at 595 nm 0,8 0,7 0,6 0,5 0,4 0,3 0,2 0,1 A595 0- 0 1 50 50 1 0.102 1- Calculate the mass of proteins contained in 50 or 100 μL of diluted extract thanks to the calibration curve (graph below), performed with serum albumin (SAB). 2- Calculate the protein concentration of undiluted enzyme extract. 2 3 5 50 50 0 50 50 100 100 1 1 1 1 0.098 0.101 0.199 0.200 2 6 8 10 SAB (ug per tube) Data: the slope of the calibration curve is 0,05 µg¹¹. 4 0 12 14 6 0 100 1 0.200 16
- A series of bovine serum albumin (BSA) was prepared and 1 mL of each solution was subjected to a Bradford assay. The increase in absorbance at 595 nm relative to the concentration of protein was plotted as shown below. Save 1.0- 0.8- 0.6- 0.4- 0.2- 0.04 0.0 0.5 1.0 2.0 2.5 1.5 BSA concentration (mg/mL) a) Using the graph, calculate the original concentration of protein present in a mixture of haemoglobin and methylene blue (diluted 1:50), which gave an absorbance of 0.20 at a wavelength of 595 nm using the Bradford assay. Show all workings. Absorbance (O.D.)In RP HPLC, one of the most common separation methods used to measure purity, strength, dosage, etc, a protein would be put into 0.1% (1000 ppm) TFA (Trifluoroacetic acid), what do you suppose this does to the protein in many cases? (Pick the BEST answer). somewhat denaturing to very denaturing oxidizes cysteine ionizes acid and base groupsWhich of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
- You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.You are studying a protein-protein interaction in 2 proteins. You decide to test both these proteins in different buffers and see if the interaction is preserved. You run the assay in the following buffers, pH 7.4, pH 7.4 with BME, pH 4.5, pH 3.5, pH 11, pH 12.5. The SDS gels from the assays are attached. a. What type of protein-protein interaction do these results suggest? b. What amino acids are most likely involved in this interaction? (Guess based on assay)Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…