GENERAL, ORGANIC, AND BIOLOGICAL CHEMIS
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ISBN: 9780134990804
Author: Laura D. Frost
Publisher: PEARSON
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Textbook Question
Chapter 10, Problem 10.88AP
Chymoirypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at a pH optimum of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?
- a. decreasing the concentration of proteins
- b. changing the pH to 3.0
- c. running the reaction at 75 °C
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4. The amino acid Asp189 lies at the base of the substrate specificity pocket in the enzyme trypsin.
a. How is this related to typsin’s substrate specificity? Briefly describe the interactions between the substrate and the Asp 189.
b. If the Asp189 was replaced with a lysine residue, how would this affect substrate specificity?
c. The scientists that actually mutated the Asp189 to a lysine analyzed the three-dimensional structure of the enzyme and found that the lysine is actually not located in the specificity pocket. Instead, the Lys side chain reaches out of the base of the pocket, rendering the pocket nonpolar. With this additional information, determine how the substrate specificity would differ in the lysine-mutated enzyme.
The initial pH of a 2M arginine solution is 14. What is the predominant structure of arginine in solution at this pH?
2. A. What is the pH of Deuterium at its isoelectric point?
B. Show the structure of this amino acid at its isoelectric point.
C. What is the charge of this amino acid in a strongly acidic solution?
Chapter 10 Solutions
GENERAL, ORGANIC, AND BIOLOGICAL CHEMIS
Ch. 10 - Prob. 10.1PPCh. 10 - Classify each of the amino acids in Problem 10.1...Ch. 10 - Prob. 10.3PPCh. 10 - Prob. 10.4PPCh. 10 - Prob. 10.5PPCh. 10 - Give the three-letter and one-letter abbreviations...Ch. 10 - Prob. 10.7PPCh. 10 - Prob. 10.8PPCh. 10 - Prob. 10.10PPCh. 10 - Prob. 10.11PP
Ch. 10 - Consider the following tripeptide: a. Circle the...Ch. 10 - Consider the following tripeptide: a. Circle the...Ch. 10 - Prob. 10.15PPCh. 10 - Prob. 10.16PPCh. 10 - Prob. 10.17PPCh. 10 - Prob. 10.18PPCh. 10 - Prob. 10.19PPCh. 10 - How many different tripeptides that contain one...Ch. 10 - Prob. 10.21PPCh. 10 - When a protein folds into its tertiary .structure,...Ch. 10 - Prob. 10.23PPCh. 10 - What type of interaction would you expect between...Ch. 10 - Prob. 10.25PPCh. 10 - Determine whether each of the following statements...Ch. 10 - Determine whether each of the following statements...Ch. 10 - Prob. 10.28PPCh. 10 - Prob. 10.29PPCh. 10 - How do beta-amyloid plaques form in a person with...Ch. 10 - List the type of attractive force disrupted and...Ch. 10 - List the type of attractive force disrupted and...Ch. 10 - Identity each of the following statements as...Ch. 10 - Prob. 10.34PPCh. 10 - Prob. 10.35PPCh. 10 - Prob. 10.36PPCh. 10 - Prob. 10.37PPCh. 10 - Prob. 10.38PPCh. 10 - Prob. 10.39PPCh. 10 - Prob. 10.40PPCh. 10 - Prob. 10.41PPCh. 10 - Describe how a substrate is drawn to an enzyme to...Ch. 10 - Which model for enzyme-substrate interaction...Ch. 10 - Describe the key difference in the lock-and-key...Ch. 10 - Prob. 10.45PPCh. 10 - Prob. 10.46PPCh. 10 - How would the following changes affect enzyme...Ch. 10 - Chymotrypsin is an enzyme located in the small...Ch. 10 - Prob. 10.49PPCh. 10 - Indicate whether each of the following describes a...Ch. 10 - Prob. 10.51APCh. 10 - Give the name and three-letter abbreviation for...Ch. 10 - Give ihe name and three-letter abbreviation for...Ch. 10 - Prob. 10.54APCh. 10 - Prob. 10.55APCh. 10 - Aspartame, which is commonly known as Nutrasweet,...Ch. 10 - Prob. 10.57APCh. 10 - Prob. 10.58APCh. 10 - Consider the amino acids glycine, proline, and...Ch. 10 - a. Draw the structure of ValAlaLeu. b. Would you...Ch. 10 - a. Draw the structure of SerLysAsp. b. Would you...Ch. 10 - Name the covalent bond that helps to stabilize the...Ch. 10 - Prob. 10.63APCh. 10 - Prob. 10.64APCh. 10 - Prob. 10.65APCh. 10 - Identify the level of protein structure associated...Ch. 10 - Prob. 10.67APCh. 10 - Prob. 10.68APCh. 10 - Prob. 10.69APCh. 10 - Describe the changes that occur in the primary...Ch. 10 - What types of covalent bonds can be disrupted when...Ch. 10 - Prob. 10.72APCh. 10 - Prob. 10.73APCh. 10 - Prob. 10.74APCh. 10 - Prob. 10.75APCh. 10 - Prob. 10.76APCh. 10 - Prob. 10.77APCh. 10 - Match the terms (1) ES, (2) enzyme, and (3)...Ch. 10 - Match the terms (1) active site, (2) lock-and-key...Ch. 10 - Prob. 10.80APCh. 10 - The enzyme trypsin catalyzes the breakdown of many...Ch. 10 - Prob. 10.82APCh. 10 - Prob. 10.83APCh. 10 - What type of interactions between an enzyme and...Ch. 10 - Prob. 10.85APCh. 10 - Prob. 10.86APCh. 10 - Prob. 10.87APCh. 10 - Chymoirypsin, an enzyme that hydrolyzes peptide...Ch. 10 - Prob. 10.89APCh. 10 - Prob. 10.90APCh. 10 - Prob. 10.91APCh. 10 - Prob. 10.92APCh. 10 - Prob. 10.93APCh. 10 - When lead acts as a poison, it can do so by either...Ch. 10 - Increasing the substrate concentration of an...Ch. 10 - Prob. 10.96APCh. 10 - Prob. 10.97APCh. 10 - Meats spoil due to the action of enzymes that...Ch. 10 - Prob. 10.99APCh. 10 - Fresh pineapple contains the enzyme bromelain,...Ch. 10 - Prob. 10.101CPCh. 10 - Prob. 10.102CPCh. 10 - How is the structure of a soap micelle (Chapter 7)...Ch. 10 - Prob. 10.104CPCh. 10 - Prob. 10.105CPCh. 10 - Prob. 10.106CPCh. 10 - What is an essential amino acid?Ch. 10 - Prob. 1IA.2QCh. 10 - Prob. 1IA.3QCh. 10 - Prob. 1IA.4QCh. 10 - Locate the side chain (R) on each amino acid...Ch. 10 - Prob. 1IA.6QCh. 10 - Prob. 2IA.1QCh. 10 - In the preceding condensation reaction, a...Ch. 10 - Prob. 2IA.3QCh. 10 - Prob. 3IA.1QCh. 10 - Lactase, the enzyme that hydrolyzes the...Ch. 10 - Prob. 3IA.3QCh. 10 - Prob. 3IA.4QCh. 10 - Prob. 3IA.5QCh. 10 - Prob. 3IA.6QCh. 10 - Prob. 3IA.7QCh. 10 - Prob. 1ICCh. 10 - Find out how oxygen binding to hemoglobin changes...Ch. 10 - Prob. 3ICCh. 10 - Find out how penicillin acts as an antibiotic.
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