Solve the peptide problem.1. Write the structure of tripeptide in which the first amino acid is Trp, thesecond one is Glu, and the third one is Asp.Mark its N- and C-ends.What is the pl area of the tripeptide (<<7, near 7, or >>7)? Explain.What is the charge of the tripeptide placed in a buffer solution with pH 9,2?Explain.How do you think, would the Xanthoprotein reaction be positive in the solutionof this peptide? Explain.

A tripeptide is composed of 3 amino acids and have 2 covalent bonds. The tripeptide given in…

Answered: Solve the peptide problem. Write the…

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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6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…
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?
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. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be: A. +2 B. +1 C. 0 D. -1 E. -2
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
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?
A. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.
4 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pI
1. Complete the table below with information about the amino acids utilized in this pro- cedure. Remember that smaller amino acids will travel further and so will amino acids that are soluble in the solvent. Table 9-1. Amino Acids Procedure AMINO ACIDS Phenylalanine Aspartic Acid Leucine Proline matemps DRAW THE MOLECULAR STRUCTURE in POLARITY (IS IT POLAR OR NONPOLAR?) odme her basalu la MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
1. Draw the peptide chain (indicate if it is solid or hatched wedges) for the following and compute for the isoelectric point. Show solution. Glycine-(L)-Arginine-(D)-Proline-(L)-Glutamic Acid
What is the difference between a peptide and a protein? 2. What type of bond is the peptide bond? Explain why the peptide bond is rigid. 3. The pentapeptide Gln-Tyr-Asn-Ala-Asp is present in human cerebrospinal fluid, and its concentration increases in demyelinating diseases. In these diseases, the myelin sheath of nerves is damaged and impairs the conduction of nerve signals. a. What is the N-terminal amino acid? b. What is the C-terminal amino acid? c. How many peptide bonds does this pentapeptide contain? From how many amino acids is this pentapeptide derived? d. Write the structure, the three-letter designation and the IUPAC name of this pentapeptide.
2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in zig-zag style, from amino to carboxy terminus, with correct stereochemistry a. Draw the predominant form at pH = 2 b. Draw the predominant form at pH = 5 c. Draw the predominant form at pH = 7 d. Draw the predominant form at pH = 12

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