2.A. Draw the chemical structure of the tripeptide CYS-ALA-SER at pH 9.0. Note: thiols also ionize SHS.B. What are the full names of these amino acids?C. How many moles of water are liberated when this tripeptide is formed by reacting 1 mole of each of the threeamino acids?D. What is the net charge on this tripeptide at pH 9.0?NOTE: there is a table of the amino acids and each of their pka, pk, and PKR values at the end Amino AcidAlanineAmine+ Arginine2.352.01Asparagine 2.02COO Aspartic Acid 2.10SHS Cysteine 2.05COO-Glutamic Acid 2.10Glutamine 2.17Glycine2.35Amine Histidine1.77Isoleucine2.322.332.18Methionine 2.28Phenylalanine 2.582.002.21Threonine 2.09Tryptophan 2.382.202.29LeucineAmine LysineProlineSerinepk Values for amino acidspk, (a-COOH)a-carboxylic acidOH → 0 TyrosineValinepk. (a-NH₂)a-amine9.879.048.809.8210.259.479.139.789.189.769.748.959.219.2410.609.159.109.399.119.72pka (side)Side chain12.483.868.004.076.1010.5310.07Amino acids with ionizable R groups (pK's)carboxylic acid COOH PK 'sother weak acids with pk'sprimary amine NH₂ pk'sweak tertiary amine N pK,

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: 2. A. Draw the chemical structure of…

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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5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
Can you please explain how to solve this problem?
The side chain of acetyl-L-lysine-OMe has a pKa=10.5 and its acid-dissociation reaction is shown below. see attachment for Question D.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
Match amino Acid R group characteristics to the biochemical bond it can form. Alanine ◆ Glycine Proline Aspartic Acid Lysine Tryptophan ◆ Methionine Threonine Asparagine Histidine A. Pi-bonding aromatic bonds B. Non-polar, contains a sulfur atom C. Non polar bonds D. Amide group bonds E. Inserts a kink (non-freely rotating bond F. Anionic group donating bonds G. Hydroxy group bonding H. Cationic group with pK = 6.0 I. No-R group - highly flexible J. Cationic group donating bond
20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?
I. Write a balanced chemical reaction, complete with chemical structures, to show the hydrolysis of iso-C to U. II. Draw the mechanism by which iso-G converts to its "minor tautomeric form complementary to U." You may propose either an acid or base catalyst. III. Draw chemical structures of the minor tautomeric form of iso-guanine (iso-G) and uracil (U), showing the non-covalent bonding (H-bonding) interactions between them.

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