Exam 9: Catalytic Strategies
Exam 1: Biochemistry: an Evolving Science50 Questions
Exam 2: Protein Composition and Structure48 Questions
Exam 3: Exploring Proteins and Proteomes50 Questions
Exam 4: DNA, RNA, and the Flow of Genetic Information50 Questions
Exam 5: Exploring Genes and Genomes50 Questions
Exam 6: Exploring Evolution and Bioinformatics48 Questions
Exam 7: Hemoglobin: a Portrait of a Protein in Action52 Questions
Exam 8: Enzymes: Basic Concepts and Kinetics50 Questions
Exam 18: Oxidative Phosphorylation50 Questions
Exam 9: Catalytic Strategies49 Questions
Exam 10: Regulatory Strategies50 Questions
Exam 11: Carbohydrates50 Questions
Exam 12: Lipids and Cell Membranes49 Questions
Exam 13: Membrane Channels and Pumps51 Questions
Exam 14: Signal-Transduction Pathways49 Questions
Exam 15: Metabolism: Basic Concepts and Design50 Questions
Exam 16: Glycolysis and Gluconeogenesis51 Questions
Exam 17: The Citric Acid Cycle47 Questions
Exam 19: The Light Reactions of Photosynthesis50 Questions
Exam 20: The Calvin Cycle and the Pentose Phosphate Pathway46 Questions
Exam 21: Glycogen Metabolism50 Questions
Exam 22: Fatty Acid Metabolism50 Questions
Exam 23: Protein Turnover and Amino Acid Catabolism49 Questions
Exam 24: The Biosynthesis of Amino Acids48 Questions
Exam 25: Nucleotide Biosynthesis50 Questions
Exam 26: Biosynthesis of Membrane Lipids and Steroids50 Questions
Exam 27: The Integration of Metabolism50 Questions
Exam 28: DNA Replication, Repair, and Recombination48 Questions
Exam 29: Rna Synthesis and Processing47 Questions
Exam 30: Protein Synthesis48 Questions
Exam 31: The Control of Gene Expression in Prokaryotes50 Questions
Exam 32: The Control of Gene Expression in Eukaryotes50 Questions
Exam 33: Sensory Systems49 Questions
Exam 34: The Immune System50 Questions
Exam 35: Molecular Motors50 Questions
Exam 36: Drug Development44 Questions
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Which of the following is an enzyme that temporarily undergoes covalent catalysis as part of its mechanism?
(Multiple Choice)
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What type of assay allows analysis of an enzyme catalyzed reaction in milliseconds?
(Multiple Choice)
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Describe the secondary and tertiary structures in domains that form P-loops and bind phosphoryl groups.
(Essay)
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The metal ion most commonly found at the active site of metalloproteases is
(Multiple Choice)
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What is the common nucleophile found in cysteine, metallo-, and aspartyl proteases?
(Short Answer)
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A-T base pairs, which contain _____ hydrogen bonds, are more easily interrupted than G-C base pairs with _______ hydrogen bonds.
(Short Answer)
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What is significant about the slow rate for myosin's hydrolysis of ATP?
(Essay)
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EcoRV cleaves cognate DNA with a specificity approximately _____ times that of non-cognate DNA.
(Multiple Choice)
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In chymotrypsin, the tetrahedral intermediate transition state is stabilized by a structural feature referred to as the "___________________" hole.
(Short Answer)
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What metal ion is frequently found in enzyme active sites that act on phosphate-containing substrates?
(Multiple Choice)
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What features of carbonic anhydrase allow the rapid hydration of carbon dioxide?
(Essay)
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What type of symmetry is created by inverted repeats in double-stranded DNA?
(Multiple Choice)
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In proteases such as papain, a ___________________ residue is activated by hydrogen-bonding to a histidine residue.
(Short Answer)
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What is the common strategy for cysteine, metallo-, and aspartyl proteases?
(Essay)
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In trypsin, the specificity pocket contains a/an ______________ residue that binds to the positive charge of the K or R residue of the substrate.
(Short Answer)
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What supports the theory that a catalytic triad strategy is a result of convergent evolution?
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Which of the following is NOT a way in which enzymes stabilize a transition state?
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