Help please 6) What is the pH of a lysine solution for scenario (a) and (b). (10 points)Amino Acid | MWpka (25 °C)pl (25° C)pKa1 pKa2 pka3Lysine146.19 2.16 9.06 10.54 9.47(a) the alpha carboxyl group is 2/3 dissociated.(b) the alpha carboxyl group is 1/2 dissociated.

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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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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.
1. Draw an approximate titration curve for lysine, given that its pKa(COOH) = 2.18, its pKa(NH3*) = 8.95, and its pka(R) = 10.53. a. What pH ranges would Lys be a good buffer at? b. What is the pl of Lys? C. Draw the structures of the predominant species in solution at (i) pH 0, (ii) pH 7, (iii) pH 9.5, (iv) pH 12.
Given the following information about amino acid tyrosine answer questions 1 & 2: A. O H HO OH HO HO рказ 10.1 H NH₂ CH₂OH A. NH3 С. НО 1. Which of the above forms of tyrosine will be predominant in a solution with pH 9.5? 2. Which of the above forms of tyrosine is a cation? Answers to Questions 3 & 4 should be selected from the following choices: CH₂OH Holl O OH B. NH₂ pka2 9.01 conj acid OH В. НО "OH D. HO HO H OH pka1 2.2 O H -OH CH₂OH C. NH3 HO NH₂ O HO OH D. 3. Which of the monosaccharides above is a non-reducing sugar? 4. Which of the monosaccharides above is an aldotetrose? 5. What is the main functional group in a protein? ||||OH
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL 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 relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
Diethylaminoethyl cellulose is a positively charged resin used in ion-exchange chromatography with a pKa is about 11. A negatively charged protein with an isoelectric point of 5.0 is applied to the column in a buffer at pH 7 and containing 0.1 M NaCl. Which of the following conditions is most likely to weaken the interaction between the protein and the resin? A Raising the pH to 8 and decreasing the NaCl to 0.05 M B Raising the pH to 8 and increasing the NaCl to 0.2 M C Lowering the pH to 6 and decreasing the NaCl to 0.05 M D Lowering the pH to 6 and increasing the NaCl to 0.2 M
What are the components of a lysine buffer at pH 9.2? Refer to the following forms of lysine: A H B H H H H;N-C-COOH H;N-C-coo- H,N-C-c0- H,N-C-coo- CH2 CH2 CH2 CH. CH2 CH, pk-2.17 pk=4.04 pk=12.48 CH, CH, ÇH2 CH, CH. CH, CH, CH. CH, CH, NH, NH, NH, NH, . A and B .C and D .B and C . A and D B and D
The amino acid glycine is often used as the main ingredient of a bufferin biochemical experiments. The amino group of glycine, which has apKa of 9.6, can exist either in the protonated form. (a) In what pH range can glycine be used as an effective buffer due to itsamino group?(b) When 99% of the glycine is in its protonated form, what is the numerical relation between the pH of the solution and the pKa of the amino group?
8) The amino acid Cysteine has this structure and pka's: SH (8.00) (10.25) H3N+ CH₂ -COOH (2.05) a) Sketch the titration curve of Cysteine (originally at pH = 0) vs. NaOH. b) At what pH is Cysteine most water soluble?
pKal 2.19 pKa2 9.67 pKa3 4.25 Amino acid Glutamic acid Threonine |Isoleucine Arginine 2.63 2.36 2.17 9.10 9.68 9.04 12.48 Draw the predominant ion of glutamic acid at its pl. Given the R group of glutamic acid is CH,CH,COOH. (ii) Draw a tripeptide of Gly-Ser-Val. Also indicate in the structure the peptide bond, N-terminus and C-terminus. (R groups for Gly, Ser, and Val is H, CH,OH and CHCH;CH; respectively).
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…
The skeletal structures of the two amino acids, glycine and lysine, are given below along with the values of the relevant acid dissociation constants (pKa). NH,* PK, - 10.79 - HạN*CH2CO,¯ S pK¸=2.35 (CH2)4 - H3N*CHCO,- pK,=9,78 lysine (Lys) glycine (Gly) pK, = 9.18 pK, - 2.16 For an aqueous solution of glycine alone, calculate the value of pH at which the ratio of the concentration of neutral glycine zwitterions to the concentration of protonated cation is 102. On your under each of the following conditions. In the blank, provide the total charge of the dipeptide. (Example: If the charge is two plus write the answer simply as 2, if the charge is negative two write the answer as -2). draw the skeletal structure of the dipeptide, Lys-Gly, when it is solvated in an aque us solution i. pH= 1 ii. pH= 12
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 3

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6) What is the pH of a lysine solution for scenario (a) and (b). (10 points) Amino Acid | MW pka (25 °C) pl (25° C) pKa1 pKa2 pka3 Lysine 146.19 2.16 9.06 10.54 9.47 (a) the alpha carboxyl group is 2/3 dissociated. (b) the alpha carboxyl group is 1/2 dissociated.