Essential Organic Chemistry, Global Edition
3rd Edition
ISBN: 9781292089034
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 17, Problem 57P
A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutant polypeptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown here. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?) (Hint: Photocopy the fingerprints, cut them out, and overlay them.)
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A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutant poly peptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown below. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?)
A. Lysine is considered a basic amino acid containing a guanidino group. If all ionizable protons from lysine were deprotonated, what will be the overall charge for the lysine?
B. Which of the following is true regarding amino acids?
-Leucine and isoleucine have the same molecular mass.
-Glycine is a chiral molecule.
-Proline is considered to be an ⍺-amino acid.
-Lysine (short for L) is a basic amino acid.
Draw out the peptide IYV and clearly label/identify all the Phi, Psi, and peptide bonds present in the peptide. Be sure to draw out the entire peptide and label the N- and C-termini. Which type of secondary structure would this peptide most likely take on (assuming it would take on a secondary structure)?.
Chapter 17 Solutions
Essential Organic Chemistry, Global Edition
Ch. 17.1 - a. Explain why, when the imidazole ring of...Ch. 17.2 - Prob. 2PCh. 17.3 - Prob. 3PCh. 17.3 - Prob. 4PCh. 17.3 - Prob. 6PCh. 17.4 - Calculate the pI of each of the following amino...Ch. 17.4 - a. Which amino acid has the lowest pI value? b....Ch. 17.5 - What aldehyde is formed when valine is treated...Ch. 17.5 - Prob. 10PCh. 17.5 - Prob. 11P
Ch. 17.5 - Prob. 12PCh. 17.6 - Prob. 13PCh. 17.6 - What amino acid would be formed using the...Ch. 17.6 - What amino acid would be formed when the aldehyde...Ch. 17.7 - Pig liver esterase is an enzyme that catalyzes the...Ch. 17.8 - Prob. 17PCh. 17.8 - Prob. 18PCh. 17.8 - Prob. 19PCh. 17.8 - Prob. 20PCh. 17.10 - Prob. 21PCh. 17.10 - Prob. 22PCh. 17.10 - Why does cyanogen bromide not cleave on the C-side...Ch. 17.10 - Prob. 24PCh. 17.10 - Prob. 26PCh. 17.12 - Prob. 27PCh. 17.13 - a. Which would have the greatest percentage of...Ch. 17 - Draw the predominant form of the following amino...Ch. 17 - What is the pI of serine?Ch. 17 - Prob. 31PCh. 17 - Prob. 32PCh. 17 - Which would have a higher percentage of negative...Ch. 17 - Draw the form of aspartate that predominates at...Ch. 17 - Prob. 35PCh. 17 - A professor was preparing a manuscript for...Ch. 17 - a. Why is the pKa of the glutamate side chain...Ch. 17 - Prob. 38PCh. 17 - Determine the amino acid sequence of a polypeptide...Ch. 17 - Prob. 40PCh. 17 - Prob. 41PCh. 17 - Three peptides were obtained from a trypsin...Ch. 17 - Prob. 43PCh. 17 - After the polypeptide shown here was treated with...Ch. 17 - The disulfide bridges of a polypeptide were...Ch. 17 - -Amino acids can be prepared by treating an...Ch. 17 - Reaction of a polypeptide with carboxypeptidase A...Ch. 17 - Prob. 48PCh. 17 - Prob. 49PCh. 17 - Show how valine can be prepared by a. a Strecker...Ch. 17 - Prob. 51PCh. 17 - Why is proline never found in an -helix?Ch. 17 - Determine the amino acid sequence of a polypeptide...Ch. 17 - Prob. 55PCh. 17 - A chemist wanted to test his hypothesis that the...Ch. 17 - A normal polypeptide and a mutant of the...
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- On complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?arrow_forward22-42 (a) How many atoms of the peptide bond lie in the same plane? (b) Which atoms are they?arrow_forwardA tripeptide undergoes complete hydrolysis and the resulting mixture contains only phenylalanine and glycine. Draw all possible sequences for the original tripeptide.arrow_forward
- a. which amino acid can form an N-linked bond with any carbohydrate b. which amino acid would most likely be found at a rigid turn in a protein structure?arrow_forwardAmino acid structure and composition: Assuming physiological pH conditions, draw the peptide backbone of a protein composed of four amino acids. The protein isa) overall positively charged.b) capable of forming disulfide bond with another protein,c) has two amino acids that can participate in hydrogen bond formation.d) one peptide bond in cis conformation must show the complete name, single letter abbreviation and structure of each amino acid. Make sure to highlight the peptide bond that is in cis conformationarrow_forwardSuppose that peptide N and O are segments in the globular protein's primary structure, where will each peptide (a. Peptide N and b. Peptide O) be most likely located - is it on the surface, completely exposed to the aqueous environment, or interior of the protein? Explain. Peptide N: L--L--F--A--I--A--M--F--L--N--I--A--I--A--I Peptide O: S--T--E--K--D--Rarrow_forward
- Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the α carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.arrow_forwardIn naming an amino acid, how may one indicate whether it is in the D or L configuration? Support answer with illustration. How are amino acids linked together in a protein molecule? Write the general structure of the tripeptide lys-phe-meth. Show their peptide bonds What is protein denaturation? Give 5 agents that can denature proteins. Is it possible for a denatured protein to revert back into its native/ original form? Explain your answer.arrow_forwardDraw an equation for the hydrolysis of a peptide bond of the polypeptide shown belowarrow_forward
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