b. You have 100 mLs of a 2 M histidine solution at pH 6.0, how many mls of a 5 M KOH solution must be added to bring the pH to exactly 7.0? Report your answer to 1 decimal point - assume no change in volume
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- b. What is the most effective buffer against bases? ____________________________________________________________________________________________________________________________________________________________________________Assuming equal concentrations of conjugate base and acid, which one of the following mixtures is suitable for making a buffer solution with an optimum pH of 7.4–7.6? NaOCl / HOCl (K a = 3.2 × 10 –8) NH 3 / NH 4Cl (K a = 5.6 × 10 –10) NaNO 2 / HNO 2 (K a = 4.5 × 10 –4) NaCl / HCl CH 3COONa / CH 3COOH (K a = 1.8 × 10 –5)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…
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- 12 grams of glucose will make how many mL of a 0.5 g/mL solution?Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 75,000 5.0 No 2 12,500 4.8 No 3 73,000 9.8 Yes a. What type of chromatography separates proteins based on their size? b. What type of chromatography separates proteins based on their charge? c. Could gel filtration chromatography be used to separate a mixture containing Protein 2 and 3? Clearly explain why or why not. If gel filtration chromatography can be used to separate Protein 2 from Protein 3, which protein would elute first (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins (Protein 2 and Protein 3) be monitored at 280nm and 400nm (clearly explain)? d. Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by…Most protein dissolve in neutral salt solution, is that true? Provide reasoning
- A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…For a weak acid with a pKa of 6.0, calculate the ratio of conjugate base to acid at a pH of 5.0* Express the strength of a solution in the form of a fraction, a ratio, and a percent if 200 mL of the solution contain 50 mL of a drug. * Express the strength of a solution in the form of a fraction, a ratio, and a percent if 8 mL of the solution contain 3 g of a drug. * How many milliliters of a 0.5% solution contain 4 grams of a drug?