Exam 24: Amino Acids, Peptides, and Proteins
Exam 1: Introduction and Review127 Questions
Exam 2: Structure and Properties of Organic Molecules129 Questions
Exam 3: Structure and Stereochemistry of Alkanes129 Questions
Exam 4: The Study of Chemical Reactions128 Questions
Exam 5: Stereochemistry128 Questions
Exam 6: Alkyl Halides: Nucleophilic Substitution and Elimination132 Questions
Exam 7: Structure and Synthesis of Alkenes128 Questions
Exam 8: Reactions of Alkenes132 Questions
Exam 9: Alkynes124 Questions
Exam 10: Structure and Synthesis of Alcohols132 Questions
Exam 11: Reactions of Alcohols124 Questions
Exam 12: Infrared Spectroscopy and Mass Spectrometry120 Questions
Exam 13: Nuclear Magnetic Resonance Spectroscopy130 Questions
Exam 14: Ethers, Epoxides, and Thioethers127 Questions
Exam 15: Conjugated Systems, Orbital Symmetry, and Ultraviolet Spectroscopy130 Questions
Exam 16: Aromatic Compounds128 Questions
Exam 17: Reactions of Aromatic Compounds129 Questions
Exam 18: Ketones and Aldehydes132 Questions
Exam 19: Amines129 Questions
Exam 20: Carboxylic Acids125 Questions
Exam 21: Carboxylic Acid Derivatives128 Questions
Exam 22: Condensations and Alpha Substitutions of Carboxyl Compounds125 Questions
Exam 23: Carbohydrates and Nucleic Acids125 Questions
Exam 24: Amino Acids, Peptides, and Proteins127 Questions
Exam 25: Lipids127 Questions
Exam 26: Synthetic Polymers128 Questions
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Which amino acid's side chain is negatively charged at biological pH?
(Multiple Choice)
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Provide the structure of the predominant form of L-methionine present in an aqueous solution at biological pH.
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What is the name of the amino acid produced when propanoic acid is subjected to the following sequence of reagents: 1. PBr3, Br2; 2. H2O; 3. NH3, Δ?
(Multiple Choice)
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Provide the major organic product in the reaction of L-methionine with benzyl chloroformate.
(Essay)
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Provide the structure of the predominant form of L-valine present in an aqueous solution at biological pH.
(Essay)
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Which of the following amino acids has a nonpolar side chain?
(Multiple Choice)
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If the side chain of asparagine is hydrolyzed, what amino acid is formed?
(Short Answer)
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Which of the following arrangements is usually not found in the secondary structure of proteins?
(Multiple Choice)
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Which of the following amino acids has a side chain which contains a nonbasic nitrogen?
(Multiple Choice)
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When a disulfide linkage is formed, the compound containing this new linkage has been ________.
(Multiple Choice)
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Bradykinin is a nonapeptide released by globulins in the blood in response to a wasp sting. Hydrolysis gives the following amino acids: 2 Arg, Gly, 2 Phe, 3 Pro, and Ser. Edman degradation gives phenylthiohydantoin of Arg. Cleavage with carboxypeptidase gives Arg. Partial hydrolysis gives the following di- and tripeptides: Phe-Ser, Pro-Gly-Phe, Pro-Pro, Ser-Pro-Phe, Phe-Arg, and Arg-Pro. What is the amino acid sequence of bradykinin?
(Short Answer)
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Which of the following reagents can be used to convert disulfide bridges into cysteic acid residues?
(Multiple Choice)
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________ of a protein usually results in the precipitation of the protein and loss of its biological activity.
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Which of the following reagents are commonly used to acylate the amino group of an amino acid?
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