Five amino acids were subjected to normal phase chromatography, and the folkowing Rf val were computed: A -0.59 B-0.12 C- 0.71 D- 0.33 E- 0.20 Which is the most polar amino acid? O A O B Oc O D
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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?Five 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?80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
- A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?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) speciesA 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 threonineYou 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.
- 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.Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…The standard curve provided below will allow you to answer the remaining questions. Generic Standard Curve 0.7 y = 0.9425x- 0.0034 0.6 0.5 0.4 0.3 02 0.1 0.1 0.2 0.3 0.4 0.5 0.6 0.7 Concentration (mg/ml) - Please describe two ways in which you could use this standard curve to determine the concentration of a pigment in an unknown sample.| #1: #2: -What is your rough estimation of the concentration if you determine the absorbance of a sample is 0.150? Absorbance
