a) Draw amino acid (L-Methionine) at low pH (pH= 1) b) Calculate the pl for amino acid Methionine
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- A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separationa) Draw amino acid (L- Cysteine) and determine the net chagre at each pH (1-3-7-10-13-) b) Calculate the pl for amino acid (Cysteine) 3. This question requires you to use an amino acid with an ionizable R group. Use the Amino Acids with lonizable R Groups chart to determine which amino acid you will be using. For student number 000123456; 2-6 and using the chart for Question 3 this corresponds to Glutamic Acid. Amino Acid 3=Z= pH 1 Draw the structure of L-amino acid 3 at the pH's in the table below and determine the net charge at each pH and the gl for amino acid 3. 10 Name of amino acid 3: 13 Cysteine Structure Net ChargeLook at the amino acid composition of a protein given in the table and click on the area in the 2D gel electrophoresis where you may expect the corresponding band. Amino acid composition M N P 7 3 11 A D E F G K R S V W Y ТОTAL: 16 2 12 14 4 1 3 7 2 11 11 10 1 164 Download Image. pH7 pH 9 pH3 200,000 116,250 97,400 66,200 45,000 31,000 21,500 14,400 ||| | |||
- You are working in the lab with a polypeptide that is present in solution at 1 mg/mL. The polypeptide sequence is Met followed by 20 repeats of SPRING. What is the polypeptide concentration in uM? You should calculate the molar mass manually based on the structures of the amino acids tr: //. com /rocOurcOs /teols lamine acid chartA 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 mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation
- In the figures are the titration curves of two amino acids. Consider the first titration. 00 000 pH 10.0 4 14.0 10 9 12.0 3 نیا 8.0 Select the pK, values of each functional group observed on the titration curve. 2 9 6.0 40 20 0.0 0.5 1.0 1.5 2.0 2.5 3.0 equivalents of [CH] Identify which amino acid is being titrated. arginine asparagine histidine lysine1. Draw an approximate titration curve of the following amino acid. Label the approximate isoelectric point of arginine on the curve and be sure to label the axis of the graph appropriately. You DO NOT need to draw the structure of this amino acid here. Pk1= 1.92, pk2=8.99 and pk3=12.48. Show your work for determining the isoelectric point. You can draw out your curve within the text box or upload a drawing. A▾ B I - I B 7Place each charge form of alanine under the pH condition where it would be the predominant form. The pK₁ values for the carboxyl group and amino group of alanine are approximately 2.3 and 9.7, respectively. pH 11 H | H₂C-C-COO NH₂ Does not occur in significant amounts at any pH
- A peptide has the sequence Glu-His–Trp–Ser-Gly–Leu-Arg-Pro–Gly The pK, values for the peptide's side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side-chain pKa glutamate 9.60 2.34 4.25 histidine 9.17 1.82 6.00 tryptophan 9.39 2.38 serine 9.15 2.21 glycine 9.60 2.34 leucine 9.60 2.36 arginine 9.04 2.17 12.48 proline 10.96 1.99 Calculate the net charge of the molecule at pH 3. net charge at pH 3:Case B: An oligopeptide has the ff amino acid composition: 2 Phe, 2 Met, 2 Glu, 1 Arg, 1 Val, 1 Leu, 1 Lys, 1 Gly, 1 Ser The reaction of the intact peptide with Sanger reagent followed by acid hydrolysis creates a derivative of Met. Specific cleavage of the intact peptide (using chymotrypsin) produces fragments with the ff sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe Question: What information do these result give about the sequence of the peptide?A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex