To set up a standard curve you would have had to set up a dilution series. Draw up a table showing what volume of protein solution and what volume of water you used to set up your tubes assuming you started with a 50 mg/ml stock solution of protein.
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- 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.Using the equation for the best-fit straight line through your data, the average absorbance of your unknown samples U1 and U2, and any dilution factors (DON’T LEAVE OUT THE DILUTION FACTOR), calculate the concentration of protein in the original unknown protein sample. y = 1.6849x + 0.0414R² = 0.9904Calculate 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 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?You obtained the following raw data when setting up a Biuret standard curve: BSA (mg/ml) Absorbancy 540nm 0 0.158 1 0.210 2 0.260 3 0.305 4 0.360 5 0.410 6 0.455 7 0.510 8 0.530 9 0.550 10 0.554 After blanking against a biuret-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.262 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).Given the following information, calculate the total activity in the undiluted protein sample. Activity of 1 ml of diluted sample = 0.5 Total volume of sample = 5 ml Dilution factor = 10 25 50.5 250 2.5
- Table 2. Volume of BSA, protein content, and absorbance readings of reference solutions Solution Volume of BSA standard solution (μL) Protein content(μg/mL) Absorbance value At 595 nm 1 0 0 0 2 10 1 0.022 3 30 3 0.065 4 50 5 0.106 5 70 7 0.178 6 100 10 0.299 7 120 12 0.380 Make a graph by plotting the absorbance values versus the BSA protein content (in μg) for theseven reference solutions. When constructing the graph, be…A. Biuret TestMix 1 mL of sample with 1 mL of 5% NaOH. Add 2 – 3 drops of 1% CuSO4. Question 1: What is the chemical equation of the reaction. Will it give positive reactions to all types of proteins? How about peptides and amino acids? Explain briefly.You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) Absorbancy 595nm 0 0.225 1 0.310 2 0.420 3 0.510 4 0.610 5 0.720 6 0.810 7 0.915 8 0.950 9 0.980 10 0.990 After blanking against a bradford-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.570 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).
- When pure hemoglobin (molecular mass of 64,000 Da) is separated by the following methods, what major molecular mass species do you expect to see? Gel filtration chromotography: Gel filtration with 6M Urea: SDS-PAGE with DDT: SDS-PAGE:You have 200 mL of a 1.5 M glucose solution. How many moles of glucose are there?When you plot the protein concentration against absorbance you expect to have a ______________ linear correlation because the ____________ the protein concentration, the ______________ absorbance.