PKG ORGANIC CHEMISTRY
5th Edition
ISBN: 9781259963667
Author: SMITH
Publisher: MCG
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Chapter 29, Problem 29.55P
Draw the amino acids and peptide fragments formed when the decapeptide A–P–F–L–K–W–S–G–R–G is treated with each reagent or enzyme: (a) chymotrypsin; (b) trypsin; (c) carboxy peptidase; (d)
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Draw the amino acids and peptide fragments formed when the decapeptide A–P–F–L–K–W–S–G–R–G is treated with each reagent or enzyme: (a) chymotrypsin; 8 pt helvetica roman (b) trypsin; (c) carboxypeptidase; (d) C6H5N = C = S.
Draw an equation for the hydrolysis of a peptide bond of the polypeptide shown below
Give the amino acid sequence of a hexapeptide that contains the amino acids Ala, Val, Ser, Ile, Gly, Tyr, and forms the following fragments when partially hydrolyzed with HCl: Gly–Ile–Val, Ala–Ser–Gly, and Tyr–Ala.
Chapter 29 Solutions
PKG ORGANIC CHEMISTRY
Ch. 29 - Prob. 29.1PCh. 29 - Problem 29.2
What form exists at the isoelectric...Ch. 29 - Problem 29.3
Explain why the of the group of an...Ch. 29 - Prob. 29.4PCh. 29 - Problem 29.5
What -halo carbonyl compound is...Ch. 29 - Problem 29.6
The enolate derived from diethyl...Ch. 29 - Problem 29.7
What amino acid is formed when is...Ch. 29 - Problem 29.8
What aldehyde is needed to synthesize...Ch. 29 - Problem 29.9
Draw the products of each...Ch. 29 - Prob. 29.10P
Ch. 29 - Prob. 29.11PCh. 29 - Prob. 29.12PCh. 29 - Problem 29.13
What alkene is needed to synthesize...Ch. 29 - Problem 29.14
Draw the structure of each peptide....Ch. 29 - Problem 29.15
Name each peptide using both the...Ch. 29 - Prob. 29.16PCh. 29 - Prob. 29.17PCh. 29 - Problem 29.18
Glutathione, a powerful antioxidant...Ch. 29 - Problem 29.19
Draw the structure of the...Ch. 29 - Problem 29.20
Give the amino acid sequence of an...Ch. 29 - a What products are formed when each peptide is...Ch. 29 - Prob. 29.22PCh. 29 - Devise a synthesis of each peptide from amino acid...Ch. 29 - Devise a synthesis of the following dipeptide from...Ch. 29 - Prob. 29.25PCh. 29 - Consider two molecules of a tetrapeptide composed...Ch. 29 - What types of stabilizing interactions exist...Ch. 29 - Prob. 29.28PCh. 29 - Draw the product formed when the following amino...Ch. 29 - With reference to the following peptide: a...Ch. 29 - Devise a synthesis of the following dipeptide from...Ch. 29 - Prob. 29.32PCh. 29 - Histidine is classified as a basic amino acid...Ch. 29 - Tryptophan is not classified as a basic amino acid...Ch. 29 - What is the structure of each amino acid at its...Ch. 29 - What is the predominant form of each of the...Ch. 29 - 29.37 What is the predominant form of each of the...Ch. 29 - a. Draw the structure of the tripeptide A–A–A, and...Ch. 29 - 29.39 Draw the organic products formed in each...Ch. 29 - 29.40 What alkyl halide is needed to synthesize...Ch. 29 - 29.41 Devise a synthesis of threonine from diethyl...Ch. 29 - 29.42 Devise a synthesis of each amino acid from...Ch. 29 - Prob. 29.43PCh. 29 - Prob. 29.44PCh. 29 - Prob. 29.45PCh. 29 - Prob. 29.46PCh. 29 - Prob. 29.47PCh. 29 - 29.48 Brucine is a poisonous alkaloid obtained...Ch. 29 - Prob. 29.49PCh. 29 - Prob. 29.50PCh. 29 - Draw the structure for each peptide: (a) Phe–Ala;...Ch. 29 - 29.52 For the tetrapeptide Asp–Arg–Val–Tyr:
a....Ch. 29 - Prob. 29.53PCh. 29 - Prob. 29.54PCh. 29 - 29.55 Draw the amino acids and peptide fragments...Ch. 29 - Prob. 29.56PCh. 29 - Prob. 29.57PCh. 29 - Prob. 29.58PCh. 29 - 29.59 An octapeptide contains the following amino...Ch. 29 - 29.60 Draw the organic products formed in each...Ch. 29 - Draw all the steps in the synthesis of each...Ch. 29 - 29.62 Write out the steps for the synthesis of...Ch. 29 - 29.63 Besides the Boc and Fmoc protecting groups...Ch. 29 - 29.64 Another method to form a peptide bond...Ch. 29 - 29.65 Draw the mechanism for the reaction that...Ch. 29 - 29.66 Which of the following amino acids are...Ch. 29 - 29.67 After the peptide chain of collagen has been...Ch. 29 - Prob. 29.68PCh. 29 - Prob. 29.69PCh. 29 - 29.70 The anti-obesity drug orlistat works by...Ch. 29 - Prob. 29.71P
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- 22-48 How many amino acid residues in the A chain of insulin are the same in insulin from humans, cattle (bovine), hogs, and sheep?arrow_forward22-97 Gelatin is derived from collagen by denaturation. Is a gelatin dessert likely to be a good source of dietary protein?arrow_forwardFor the tripeptide GlyAlaCys a. What amino acid is located at the peptides N-terminal end? b. What amino acid is located at the peptides C-terminal end? c. How many peptide bonds are present? d. How many amide linkages are present?arrow_forward
- 22-104 Why is collagen not a very good source of dietary protein?arrow_forwardConsider the tripeptide leucylvalyltryptophan. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has a basic side chain?arrow_forward22-44 How can a protein act as a buffer?arrow_forward
- Consider the tripeptide tyrosylleucylisoleucine. a. Specify its structure using three-letter symbols for the amino acids. b. How many peptide bonds are present within the peptide? c. Which of the amino acid residues has the largest R group? d. Which of the amino acid residues, if any, has an acidic side chain?arrow_forward22-91 Which amino acid does not rotate the plane of polarized light?arrow_forward14. (a) Identify the acetal and the ketal group in the following disaccharide. (b) Decide whether the compound is a non-reducing or reducing sugar. OH НО HƠ HO Н HO Н НО HO 15. (a) Identify the glycosidic bond in the following disaccharide. (b) Decide whether the compound is a non-reducing or reducing sugar. (c) Polysaccharide units are usually bonded together with a or B 1, 6 or 1, 4 linkages. What linkage is used in the disaccharide shown below? s) НО НО НО HO НО -OH OH -H OH CH2OH 16. Draw the structure for 1,4-B-D-galactopyranosyl-D-glucose. ( но- 17. Assign an R/S designation to each chirality center in the following compound: ( CHO НО -OHarrow_forward
- 4arrow_forwardAn enzyme catalyzes the hydrolysis of an ester with a certain activity, but this activity is lost in a 3 M urea solution. What is the most likely explanation for the loss of activity? (A) Urea binds to the active site of the enzyme competitively with the substrate. (B) Urea causes the cleavage of the peptide bonds in the enzyme. (C) Urea causes the enzyme to denature and lose its specific three-dimensional shape. (D) Urea reacts with disulfide bonds in the enzyme.arrow_forwardAll amino acids share a common structure, a central (alpha) carbon with four groups attached. Which of these is NOT one of the four groups attached to the alpha- carbon? O an R group an ammonium group (-NH3+) O a carboxylate group (-COO) a hydronium grouparrow_forward
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