Q2.1 1. IDraw the amino acids Asn and His and show the most prevalent interaction thatwould occur between the R-groups at pH 5. To show the interaction, use a dotted line between theatoms that are interacting and label the interaction. You can draw the two amino acids asseparate molecules or as part of a peptide. Whatever you do, you must have the proper chargeson all functional groups. Label the interaction!Draw the dipeptide Thr-Lys as it would occur at pH 7. Make sure to show the properorientation of R groups with respect to the peptide bond.2.

Asparagine is a polar uncharged amino acid, while histidine is a polar charged amino acid.…

Answered: 1. I Draw the amino acids Asn and His…

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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29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.57
1. a. Draw the following pentapeptide: lysine-leucine-aspartate-threonine-phenylalanine b. Label the amino and carboxyl terminus of your peptide c. Label each amino acid residue with one and three letter abbreviations d. Label the alpha carbons e. Label the bonds around which phi and psi rotational angles occur f. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is most likely to be acetylated?
1. What will happen if there is a change in the configuration of a protein molecule? Provide an example. 2. Give the IUPAC name for Ala-Gly-Leu
1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)
1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
1. 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 7
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
4. A. Draw the structure of the following peptide sequence at pH 2.0: ASP-ALA-THR-LYS-GLY B. What is the net charge of this pentapeptide at pH 2.0?
Which of the following is incorrect about the peptide Arg-Asp-Cys-Tyr-Gln-Arg-Glu? O a. Its estimated MW is 770 Da b. None; all the other choices are correct OC. At pH 7, it has a net charge of zero O d. At pH 7, it has six charged groups
7. Identify the primary structure of a hexapeptide containing five different amino acids if the following smaller peptides are among the partial hydrolysis products: Gly-Cys, Ala-Ser, Ala-Gly, and Cys-Val-Ala
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:
Determine the net charge of the peptide below at pH 7 and 12. Show your solution. Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys

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