Exam 6: Proteins: Three-Dimensional Structure
Exam 1: Introduction to the Chemistry of Life56 Questions
Exam 2: Water59 Questions
Exam 3: Nucleotides, Nucleic Acids, and Genetic Information68 Questions
Exam 4: Amino Acids68 Questions
Exam 5: Proteins: Primary Structure68 Questions
Exam 6: Proteins: Three-Dimensional Structure60 Questions
Exam 7: Protein Function Part I: Myoglobin and Hemoglobin74 Questions
Exam 8: Carbohydrates66 Questions
Exam 9: Lipids and Biological Membranes59 Questions
Exam 10: Membrane Transport50 Questions
Exam 11: Enzyme Catalysis53 Questions
Exam 12: Enzyme Kinetics, Inhibition and Control55 Questions
Exam 13: Biochemical Signaling50 Questions
Exam 14: Introduction to Metabolism52 Questions
Exam 15: Glycogen Metabolism and Gluconeogenesis50 Questions
Exam 16: Glucose Catabolism50 Questions
Exam 17: Citric Acid Cycle50 Questions
Exam 18: Electron Transport and Oxidative Phosphorylation50 Questions
Exam 19: Photosynthesis50 Questions
Exam 20: Lipid Metabolism51 Questions
Exam 21: Amino Acid Metabolism50 Questions
Exam 22: Mammalian Fuel Metabolism: Integration and Regulation50 Questions
Exam 23: Nucleotide Metabolism50 Questions
Exam 24: Nucleic Acid Structure50 Questions
Exam 25: Dna Replication, Repair and Recombination50 Questions
Exam 26: Transcription and Rna Processing50 Questions
Exam 27: Translation49 Questions
Exam 28: Regulation of Gene Expression50 Questions
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In a protein, the most conformationally restricted amino acid is ______; the least conformationally restricted is ______.
Free
(Multiple Choice)
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Correct Answer:
C
Which of the following structural proteins has the greatest elasticity?
Free
(Multiple Choice)
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Correct Answer:
D
Which statement below does not describe fibrous proteins?
Free
(Multiple Choice)
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Correct Answer:
A
Matching
-The overall arrangement of the regular structural elements such as the α helix and the β sheet in the protein are considered the protein's ______.
(Multiple Choice)
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Matching
-A rigid, planar structure between at least two amino acids consisting of about 40% double bond character is characteristic of a ______.
(Multiple Choice)
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The Protein Data Bank (PDB)is a database provides structural information about proteins that may be useful for which of the following?
I.A researcher studying the changes in protein fold associated with prions.
II.A researcher classifying structural elements by function.
III A researcher designing a compound to bind tightly to a particular region in the protein.
(Multiple Choice)
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Noncovalent interactions account for the strength of which of the following structural proteins?
(Multiple Choice)
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Which of the following amino acids combinations have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein?
(Multiple Choice)
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Which of the following best describes the cause of Creutzfeld-Jakob Disease (a disease which human can develop with symptoms similar to those of mad cow disease)?
(Multiple Choice)
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Of the following, which amino acid is most likely to be found in position 1 or 4 on α keratin?
(Multiple Choice)
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What observation about protein refolding or renaturation helped to solidify the connection between primary amino acid sequence and 3-D structure?
(Multiple Choice)
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Matching
-The strength of _______ comes from close packing of glycine residues and the characteristics of hydroxyproline allowing formation of a left- handed helical conformation which combines with two other left handed structures to form a right-handed triplet helix.
(Multiple Choice)
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The low pH found in the gut can enhance the digestibility of dietary protein by causing ___.
(Multiple Choice)
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Which of the following is true regarding crystalline proteins?
(Multiple Choice)
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Molecular chaperones bind to unfolded or partially folded polypeptide chains in order to accomplish which of the following?
(Multiple Choice)
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Matching
-Repeating values of and make up predictable orientations of amino acid with a chain, this predictable orientation forms___________.
(Multiple Choice)
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Imagine that a researcher treated a protein with a high concentration of a chaotropic agent.Which of the following is the most likely result of the treatment?
I.Nonpolar portions of the protein become more soluble.
II.The protein begins to denature ,
III.The protein stability increases due to hydrophobic collapse,
(Multiple Choice)
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Matching
-A historical experiment exploring denaturation upon β- mercaptoethanol reduction of disulfide bonds and spontaneous renaturation upon dialysis to remove the β- mercaptoethanol was carried out using the protein ______.This experiment demonstrated the importance of disulfide bonds and amino acid sequence in folding of proteins.
(Multiple Choice)
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Which of the following statements is true regarding collagen?
(Multiple Choice)
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