Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
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Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
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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.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 2.5Using 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 = 0.9904
- 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?When performing a separation by ion-exchange chromatography, the rate of elution of an amino acid is influenced by three main factors: a. Temperature b. Solution (buffer) pH c. Ionic strength (buffer concentration) of the eluent Briefly, explain how each of these parameters influences elution rate. Please provide only typed answer solution no handwritten solution needed allowedIf you added three proteins (Protein A, pI 5.0; Protein B, pI 6.0; Protein C, pI 7.0) to an anion exchange column equilibrated with bicine buffer, pH 8.5, in what order would these protein be expected to elute as the column was loaded, washed, and then increasing amounts of NaCl were added?
- 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?When comparing the biuret reaction to measuring protein absorbance directly at 280 nm, list two benefits of utilizing the biuret reaction to quantify protein concentration.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.
- Student A says that he can insert any value of optical density in the equation of standard curve to determine the corresponding value of protein content. Does the student say it right or wrong? Explain why?You have given two proteins with a pI of 4.5 and pI of 7.7? Using an anion-exchange column, how can these two proteins be separated. What buffer could you prepare?You are given two proteins with a pI of 4.5 and pI of 7.7. In an example of an anion-exchange column, can you use a buffer to separate these two proteins? What buffer protein can be used to separate the two proteins mentioned above?