You obtained the following raw data when setting up a Biuret standard curve: BSA (mg/ml) 0 1 2 3 4 5 6 7 8 9 10 Absorbancy 540nm 0.158 0.210 0.260 0.305 0.360 0.410 0.455 0.510 0.530 0.550 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 0.336 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).
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- You obtained the following raw data when setting up a Bradford standard curve: Absorbancy BSA (mg/ml) 595nm 0.225 1 0.310 2 0.420 0.510 4 0.610 0.720 6 0.810 0.915 8 0.950 0.980 10 0.990 After blanking against a bradford-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.594 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).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).You obtained the following raw data when setting up a Biuret standard curve: Absorbancy BSA (mg/ml) 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 10 0.550 0.554 After blanking against a biuret-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.284 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).
- 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).Using the data from the standard curve done previously, you record the absorbance of your extracted milk protein sample at 0.499 at 540nm. What is the mass of the protein in mg assuming you collected 10mL worth of the protein? Your standard curve should have a line of best fit with the equation y=0.0001x+0.0038.Viscosity measurements were done on native form of Protein XYZ and on 4 denaturants. The crude Protein XYZ was diluted to produce 5% w/v. Using the Ostwald viscometer, the following data were obtained: time, sec time, sec time, sec time, sec Denaturant Blank (Native) Native Blank (Denaturant) Denatured pH= 2.00 70 95 70 101 Temp (90 °C) 70 98 70 150 0.1M Urea 72 97 88 110 DTT 71 96 90 170 a. Calculate and tabulate the reduced viscosities (in mL/g) of the native and denatured Protein XYZ. b. Determine two most effective denaturants. c. What can be inferred with the two most effective denaturants? Dont reject if you dont know the answer!
- The calibration curve shown below was used to analyze an unknown protein solution. What is the concentration of the unknown solution, if the absorbance of the unknown is 0.505? Answer in ug/mL. 1.2 y%3D0.005x+0.061 R=0.992 0.8 0.6 0.4 0.2 50 100 150 200 250 Concentration ug/ml AbsorbanceA mixture containing only KCl and NaBr is analyzed by the Mohr Method. A 0.3172-g sample is dissolved in 50 mL water and titrated to the Ag2CrO4 endpoint, requiring 36.85 mL of 0.1120 M AgNO3. A blank titration requires 0.71 mL of titrant to reach the same endpoint. Report the % (w/w) KCl and NaBr in the sample. [Ans . 84.41 % (w /w); 17.59 % (w /w)]Solution Absorbance mg/ml aspirin Standard solution - 1.6 mg/mL A 0.638 0.08 mg/mL B 0.504 0.064 mg/mL C 0.376 0.048 mg/mL D 0.259 0.032 mg/mL E 0.126 0.016 mg/mL A = -log T where T = %T ÷ 100 Construct a callibration curve using the above data. Absorbance should be on the vertical axis and "mg/mL of acetylsalicylic acid" on the horizontal axis. The line should go through the origin. Using the data provided, the graph you have generated, and the procedure that was used to generate the solutions which were examined by spectroscopy, calculate the amount of acetylsalicylic acid per tablet. Commercial tablet 1 labelled as 100 mg enteric coated Absorbance = 0.16 Commercial tablet 2 labelled as 300 mg Absorbance = 0.45 Student prepared tablet from practical 5 Absorbance = 0.19 Using the data provided, the graph you have generated, and the procedure that was used…
- You just made a 1.5M permanganate solution. What concentration is your potassium permanganate solution in percent? "K: 39.10 g/mole" "Mn: 54.94 g/mole" "O: 16 g/mole" "MW of KMnO4 is 158.04 g/mole" O a. 0.24% Ob. 20.1% O c. 15.8% O d. 23.7% O e. 2%The 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?The glucose content of samples can be determined using Nelson't test. The equation of the line for the standard curve preapred for varying concentrations of glucose is y = 3.0x + 0.2. Based from this information, determine the glucose concentration (in M) of a strawberry preserve having an absorbance reading of 1.35.