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.
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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.
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- A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?The following stock solutions are available to make a protein extraction buffer: 100% Nonidet P-40, 1 M Tris-Cl, and 0.5 M EDTA. What quantity of the original stocks will be needed to make 250 ml of buffer with the following final concentrations: 0.5% Nonidet, 150 mM Tris-Cl, and 10 mM EDTA?To 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?
- 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 2.5A mixture of three proteins was subjected to ion exchange chromatography using CM-cellulsoe as the stationary phase. The elution buffer had a pH of 7.5. Proteins were eluted by increasing the ionic strength of the buffer. Predict the order of elution of the following proteins:Pepsinogen, pI = 1Cytochrome c, pI = 10.6Myoglobin, pI = 6.8A researcher prepares 100 mL of aqueous solution containing 0.1 g of a protein. The researcher then uses an experimental apparatus ,where he notes that, at room temperature (300K) and atmospheric pressure (101.325 kPa), distilled water flows naturally into the solution compartment. However, when he applies an extra pressure of 1000 Pa he observes that the flow of distilled water ceases and the system is in balance. Calculate the molar mass of this protein, in kDa (1 Da = 1 g/ mol); Why does the flow of distilled water cease with the application of the pressure of 1000 Pa? Explain in terms of potential chemicals. %3D
- Calculate the concentration of 0.2ml amino acid when path length is 1cm and has an absorbance value of 0.50, if a 0.5ml solution of same amino acid has a concentration of 0.72mg/ml with an absorbance of 0.9.A mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase TransferrinCalculate the concentration of the unknown protein in mg/ml.
- 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.An ion-exchange chromatographic separation is performed using a diethyl-aminoethyl- (DEAE)-sepharose column to separate proteins in a mixture. The mixture contains Protein A (pl=6.0), B (pl35.0), C (pl=7.5), D (pl =1), and E (pl=4.0). The protein mixture is prepared in a buffer solution pH =5. When the protein mixture is loaded onto the column, and the column is washed with a buffer solution pH 5, which protein(s) will be captured by DEAE-sepharose in the column? O Protein B because it is predominantly in net negative charge form. O Proteins D and E because they have predominately net negative charge in pH 5 solution O Proteins A, C, D and E because they have charges O Proteins A and C because both both predominantly have net positive charges O Proteins Band E because both predominantly have net positive chargesThe 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 Absorbance