Refer to the following titration curve below:13121110765446 81012141618202224262830Volume of Titrant / mL- Unknown Acid 0.10 mol/L - titrant = NaOH 0.1 mol/LWhat is the isoelectric point of histidine, according to thetitration curve? Input your answer until the first decimal point.2.9,

Iso electric point: the pH at which the Amino acid exists in a zwitter ionic state us called iso…

Answered: Refer to the following titration curve…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Refer 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+
Use the provided theoretical titration curve of histidine in answering the questions asked. pH 14 12 10 8 6 4 2 O 0 2 4 1. In the titration curve above, what is the isoelectric point of histidine? Make sure to place your answer up until the first decimal point. 6 8 10 12 14 16 18 20 22 24 26 28 30 32 34 36 38 40 Volume of Titrant / mL Histidine 0.10 mol/L - titrant = NaOH 0.1 mol/L 2. Which form of histidine is the most abundant at pH 10.0? (and why) a. Hist b. His c. His2+ d. His 3. True or False: All amino acids have zwitterions (explain) 4. Which of the following forms of Histidine is/are amphoteric? (More than one answer may apply) (explain) a. Hist b. His c. His2+ d. His
2. 0.1 mL of a protein solution of concentration of 7 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 3 mL of this solution was then mixed with 27 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
Calculate the unknown concentration of the PROTEIN C with an absorbance value of A412 given the standard curve indicated in the table below. Write your final answer (NUMBER ONLY) in two decimal places rounded off. Protein concentration (µg/mL) 0 0.02 0.04 0.06 0.08 0.10 Your answer APIENT Absorbance 0.000 0.161 0.284 0.438 0.572 0.762
The amino acid arginine ionizes according to the following scheme: NH₂ I C=N I ΝΗ Part A pl = Submit H (CH₂)3 H-N-C-COOH II HH 1 [ΠΙ ΑΣΦ H H Calculate the isoelectric point of arginine. Express your answer using three significant figures. Request Answer pk-2.17 -H* +H* wwwww NH₂ C=N ΝΗ H (CH₂)3 1 ? H H-N-C-COO- | | H H 11 H pk-8.99 -H* +H* NH₂ I C=N I ΝΗ T (CH₂)3 H H H₂N-C-COO- I H pk - 12.5 -H* +H* NH₂ C=N=H NH I (CH₂)3 H₂N-C-COO- I H IV
Highlight your values of A,B,C and D. For your question: A mL of B mol/L sodium phosphate solution is combined with C mL of D mol/L calcium bicarbonate. (Calcium bicarbonate is soluble.) A mL B mol/L C mL D mol/L 75.0 ml 0.300 67.5 0.350 Before you begin your reaction, you must accurately produce 1.500 L of your sodium phosphate solution from sodium phosphate trihydrate solid. Write out a procedure to explain all the steps you will take in the lab when making the solution to ensure that your solution concentration is accurate. Please include calculations that show the required mass of solid. Also include the correct names of all equipment used.
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
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.
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.
Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly w/ isoelectric focusing?
A solution of Na2CO3 contains 53g of solute in 200ml of solution. What is the molarity of this solution.
Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…

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