A researcher is preparing a reaction mixture to test the activity of a protein. They combine at room temperature the required reaction components, which contained in a final 150 ml volume 200 mM NaCl and unknown concentrations of weak acid and conjugate base of a buffer compound. They are using a pH meter to determine the acidity of the solution and observe the following pH value that is displayed by the device. Can you determine the hydrogen ion [H+] concentration of the solution? Provide the value with three decimal places and an appropriate unit in the answer box. Note: You may need to round the numbers to get the required answer. 3.35
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- A researcher is preparing a reaction mixture to test the activity of a protein. They combine the required reaction components, which contained in a final 100 ml reaction volume 200 mM NaCl, unknown concentrations of acetic acid and acetate anions and a total [H+] concentration of 790 ricromolar. Can you determine the pH of the solution? Provide the answer to one decimal place. Note: You may need to round the numbers to get the required answer. 100 Strips pH indicator strips non-bleeding pH pH 0-14 EM-Reagents Dip in-read while still moist. immerse in weakly-buffered solutions une there is no further color change (1-10 min) 3 7 5 6Given 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.A 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
- 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!amino glycine pka is 2.4, 9.8 Calculate the most effective buffering range. if there is two pka, since there are 2 buffer region, is the buffering range 1.4~3.4 and 8.8~10.8? i would like to know the correct answer and detailed solution/reason.A 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 = 6.8
- 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 2.5Calculate the volume of TAE buffer that you will need to prepare a 100ml solution of 1X strength if you only have a 50X concentrated solution available.You need a buff er at pH 7.5 for use in purifying a protein at 4°C. You have chosen Tris, pK 8.08, ΔH° = 50 kJ · mol−1. You carefully make up 0.01 M Tris buffer, pH 7.5 at 25°C, and store it in the cold to equilibrate it to the temperature of the purifi cation. When you measure the pH of the temperature-equilibrated buff er it has increased to 8.1. What is the explanation for this increase? How can you avoid this problem?
- N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic acid) buffer at pH 7 with 400 mM NaCl. A A purified protein is in a Hepes dialysis membrane tube holds a 5.0 mL sample of the protein solution. The sample tube floats in a beaker containing 0.50 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na*, CI", and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. Calculate the final NaCl concentration in the 5.0 mL protein sample after dialysis in 300 mL of the same Hepes buffer, with 0 mM NaCl, twice in succession. [NaCl] after a single dialysis: [NaCl] after a double dialysis: mM mMHow much of the enzyme proteinase k (solute) is required to make 250ml of a solution with a concentration of .01mg/ml? (Weight/volume ratio)You need to make a protein buffer of: . • • 100 mM NaCl 25 mM Tris 8 5% w/v glycerol • 2 mM DTT Your stock solutions are: 5 M NaCl • 2 M Tris 8 • 70% w/v glycerol • DTT @ 154.25 g/mol How would you make a 1L protein buffer Solution? Show your work and describe.