Essential Organic Chemistry, Global Edition
3rd Edition
ISBN: 9781292089034
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Textbook Question
Chapter 17, Problem 44P
After the polypeptide shown here was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.)
Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-
Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp
- a. After a polypeptide is treated with maleic anhydride, why does trypsin no longer cleave it on the C-side of lysine?
- b. How many fragments are obtained from the polypeptide?
- c. In what order would the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
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After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhy-dride, trypsin will cleave the polypeptide only on the C-side of arginine.)
Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp
After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-GlyArg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp a. After a polypeptide is treated with maleic anhydride, why does trypsin no longer cleave it on the C-side of lysine? b. How many fragments are obtained from the polypeptide? c. In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.)
Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp
After a polypeptide is treated with maleic anhydride, why does trypsin no longer cleave it on the C-side of lysine?
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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- After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp How many fragments are obtained from the polypeptide?arrow_forwardExplain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is thenitrogen that accepts the proton. 2 H+ + NH2NHCH2CH2CH2CHNH +NH3CO−O CO−O H2NC NHCH2CH2CH2CHarrow_forwardDraw the structure of the N-phenylthiohydantoin formed by initial Edman degradation of each peptide: (a) Ala–Gly–Phe–Phe; (b) Val–Ile–Tyr.arrow_forward
- Draw three-dimensional representations of the following amino acids.(a) l-phenylalanine (b) l-histidine (c) d-serine (d) l-tryptophanDraw three-dimensional representations of the following amino acids.(a) l-phenylalanine (b) l-histidine (c) d-serine (d) l-tryptophanarrow_forwardDraw the reaction for the Edman degradation product (PTH-amino acid) of the first amino acid residue in the following polypeptide chain: Cys-Leu-Val-Iso.arrow_forwardIndicate the peptides produced from cleavage by the indicated reagent: a. His-Lys-Leu-Val-Glu-Pro-Arg-Ala-Gly-Ala by trypsin b. Leu-Gly-Ser-Met-Phe-Pro-Tyr-Gly-Val by chymotrypsinarrow_forward
- What type of interaction (IMF) would be present between side chains of the following amino acid residues? Explain your answers. a) 2 phenylalanine residues b) Methionine and valine residues c) Glutamate and arginine residuesarrow_forward(a) What products are formed when each peptide is treated with trypsin? (b) What products are formed when each peptide is treated with chymotrypsin?a. Gly–Ala–Phe–Leu–Lys–Alab. Phe–Tyr–Gly–Cys–Arg–Serc. Thr–Pro–Lys–Glu–His–Gly–Phe–Cys–Trp–Val–Val–Phearrow_forwardDraw the structure of below peptide. Label the N-terminal and C-terminal amino acids and all amide bonds. M–A–T–Tarrow_forward
- An oligopeptide, 6 amino acids in length, was subjected to acid hydrolysis and yielded equimolar amounts of the following amino acids (in alphabetical order): Arg Gln Lys Met Thr Tyr Based on the following separate treatments, which amino acid is in position #5 of this sequence? a. Cyanogen bromide treatment had no effect. b. Trypsin treatment yielded a dipeptide, a tripeptide and free arginine. The tripeptide had a net positive charge at pH 7. c. Chymotrypsin treatment yielded a dipeptide and a tetrapeptide. The dipeptide had a net charge of zero at pH 5. d. The phenylthiohydantoin derivative released by one round of Edman degradation was PTH-Thr.arrow_forwardAnswer the following questions about the amino acid whose Fischer projection formula is a. Is it a D-amino acid or an L-amino acid? b. Is it a nonpolar or polar amino acid? c. Is it an essential or nonessential amino acid? d. Is it a standard or nonstandard amino acid?arrow_forwardFollowing is the primary structure of glucagon, a polypeptide hormone of 29 amino acids. Glucagon is produced in the -cells of the pancreas and helps maintain blood glucose levels in a normal concentration range. Which peptide bonds are hydrolyzed when this polypeptide is treated with each reagent? (a) Phenyl isothiocyanate (b) Chymotrypsin (c) Trypsin (d) BrCNarrow_forward
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