Refer to the following titration curve below: 13 12 11 10 7 5 4 3 2 4 6 10 12 14 16 18 20 22 24 26 28 30 Volume of Titrant / ml - Unknown Acid 0.10 mol/L - titrant = NaOH 0.1 mol/L How many buffering regions are present in the titration curve of the amino acid?
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- 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 2.5Consider the following pH titration curve of a diprotic acid. What is the approximate values for pka 1 and pka 2? the curve is attached below.1.2. Using DEAE-cellulose as ion exchange resin, indicate the starting and ending pH for the narrowest experimental pH range used to separate an amino acid mixture consisting of Cys, His and Leu Starting pH: _____ Ending pH: _____
- Using this data, calculate the molarity of the oxalic acid standard solution.In biochemistry, what is definition of buffer , which amino acid can act as buffer? what is buffer pH range?The greatest buffering capacity at physiological pH would be provided by a protein rich in which of the following amino acids? Choose one from among the possible answers and explain. Serine Cysteine Alanine Histidine
- 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…Three buffers are made by combining a 1M solution of acetic acid and a 1M solution of sodium acetate in the ratios shown in the table below. Which of these statements is true regarding the prepared buffers? (Ka= 1.7x10-5) pH of buffer 1 < pH of buffer 2 < pH of buffer 3 pH of buffer 1 = pH of buffer 2 = pH of buffer 3 pH of buffer 1 > pH of buffer 2 > pH of buffer 3 pH of buffer 1 = pH of buffer 2 > pH of buffer 3 pH of buffer 1 > pH of buffer 2 = pH of buffer 3Using 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
- Is lysine a suitable buffer at acidic, neutral, or basic pH range, and why?In an experiment, what happens to the calculated molar mass after waiting an hour between thawing the frozen cyclohexane and adding the unknown compound, during which time some of the cyclohexane evaporated. Will the molar mass be too large, too small, or unaffected? Explain.|Explain in general why the two phenomena of salting in and salting out increase the solubility or deposition of proteins and compare the strength of different salts. (Hoffmister series)