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Five amino acids were subjected to normal phase chromatography, and the following Rf values were computed:
A - 0.59
B - 0.12
C - 0.71
D - 0.33
E - 0.20
Which is the most polar amino acid?
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- Five amino acids were subjected to normal phase chromatography, and the folowing Rf values were computed: A 0.59 В - 0.12 C- 0.71 D- 0.33 E - 0.20 Which is the most polar amino acid? O A O BFive amino acids were subjected to reverse phase chromatography, and the following Rf values were computed: A - 0.23 B - 0.08 C - 0.54 D - 0.74 E - 0.96 Which is the most polar amino acid?A 100 ml solution of 0.1 M amino acid (AA) at ph 1.0 was titrated with NaOH solution. The pH was monitored, and the results were plotted on the graph. The keypoints in the titration are designated I to VII. What is the possible identity of the amino acid? What is the isoelectric point of AA? what is the pKa corresponding to the dissociation of the alpha carboxylic group? Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) species
- A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).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 chargesMr. Bibo analyzed a mixture of amino acids using thin layer chromatography where the stationary phase is a silica-coated plate. For the mobile phase, he used 50% ethyl acetate in hexane. The mixture contained three (3) amino acids whose structures are shown below. HO. HO NH2 HO, HO. NH2 NH2 Phenylalanine Threonine Aspartic acid a.) From the amino acids listed above, identify spots A, B, C, and D in the chromatogram below. BO CO b.) Threonine can be phosphorylated using an enzyme called protein kinase. The reaction is shown below. Given the same conditions Mr. Bibo used in his analysis, will the phosphorylated threonine have a higher, smaller, or the same Rf value compared to threonine? Explain in one sentence. АТР ADP CH3 CH3 Protein kinase он он NH2 NH2 Threonine Phosphorylated threonine
- You are given 0.7 M solution of the amino acid Lysine.pK1 (α-carboxyl group) = 2.18pK2 (α- amino group) = 8.95 andpK3 (Side chain) = 10.53Answer the following questions. Determine the pH of the solution if you add 26 mL 0.3 M HCl to 12 mL of the 0.7 M Lysine. Assume that Lysine is in isotonic state. Show all calculations.An enzyme (molecular weight= 24 kDa, pI= 5.5) is contaminated with two other proteins, one witha similar molecular mass and a pI of 7.0 while the other has a molecular mass of 100 kDa and a pIof 5.4. Suggest how the contaminated enzyme can be purified.Please provide a chromatography technique to isolate the protein A from the mixture containing protein A and B (shown as below). And explain the separation mechanism related to this example. Protein A: MKRHRRKKHHRKRRKKRKGH (positively charged) Protein B: MDEEEEDDDEEDDEEDEDEED (negatively charged)
- You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer in mg/ml.A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G 3Refer to the following titration curve below: 13 12 11 10 9 7 6 5 4 3 4 6 8 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 At ph 10.0, which form of histidine is most abundant? His2+ His- His° His+