Exam 6: The Three-Dimensional Structure of Proteins
Exam 1: The Scope of Biochemistry17 Questions
Exam 2: The Matrix of Life: Weak Interactions in an Aqueous Environment25 Questions
Exam 3: The Energetics of Life25 Questions
Exam 4: Nucleic Acids28 Questions
Exam 5: Introduction to Proteins: the Primary Level of Protein Structure25 Questions
Exam 6: The Three-Dimensional Structure of Proteins24 Questions
Exam 7: Protein Function and Evolution27 Questions
Exam 8: Contractile Proteins and Molecular Motors19 Questions
Exam 9: Carbohydrates: Sugars, Saccharides, Glycans28 Questions
Exam 10: Lipids, Membranes and Cellular Transport25 Questions
Exam 11: Enzymes: Biological Catalysts24 Questions
Exam 12: Chemical Logic of Metabolism25 Questions
Exam 13: Carbohydrate Metabolism: Glycolysis, Gluconeogenesis, Glycogen Metabolism, and the Pentose Phosphate Pathway41 Questions
Exam 14: Citric Acid Cycle and Glyoxylate Cycle25 Questions
Exam 15: Electron Transport, Oxidative Phosphorylation, and Oxygen Metabolism24 Questions
Exam 16: Photosynthesis26 Questions
Exam 17: Lipid Metabolism I: Fatty Acids, Triacylglycerols, and Lipoproteins26 Questions
Exam 18: Interorgan and Intracellular Coordination of Energy Metabolism in Vertebrates22 Questions
Exam 19: Lipid Metabolism Ii: Membrane Lipids, Steroids, Isoprenoids, and Eicosanoids25 Questions
Exam 20: Metabolism of Nitrogenous Compounds I: Principles of Biosynthesis, Utilization, and Turnover25 Questions
Exam 21: Metabolism of Nitogenous Compounds II: Amino Acids, Porphyrins, and Neurotransmitters25 Questions
Exam 22: Nucleotide Metabolism25 Questions
Exam 23: Mechanisms of Signal Transduction24 Questions
Exam 24: Genes, Genomes and Chromosomes25 Questions
Exam 25: DNA Replication25 Questions
Exam 26: DNA Restructuring: Repair, Recombination, Rearrangement, Amplification25 Questions
Exam 27: Information Readout: Transcription and Post-Transcriptional Processing25 Questions
Exam 28: Information Decoding: Translation and Post-Translational Protein Processing28 Questions
Exam 29: Regulation of Gene Expression25 Questions
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Which of the following would contribute to tertiary structure?
Free
(Multiple Choice)
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Correct Answer:
E
Which of the following is a highly compact structure that is very commonly used to transition from one region of secondary structure to another in a globular protein?
Free
(Multiple Choice)
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Correct Answer:
B
The two amino acids most often found in a polyproline II helix are proline and _______.
Free
(Multiple Choice)
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Correct Answer:
B
Which of the following is considered a dead-end complex (and therefore dangerous due to its resistance to proteolytic cleavage)in the protein-folding pathway?
(Multiple Choice)
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If a peptide was composed entirely of -helical structure and found to contain an integer number of complete turns, which of the following would be a possible number of amino acid residues in the peptide?
(Multiple Choice)
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Of the following proteins that aid in the folding process, which is exclusively involved in the interconversion of cis and trans bonds?
(Multiple Choice)
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In an -helix, a hydrogen bond is formed between the carbonyl oxygen of the ith residue and the amide hydrogen _____ residues away
(Multiple Choice)
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Which of the following statements regarding structural proteins is true?
(Multiple Choice)
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The presence of a hydrophobic amino acid at every third or fourth residue in -keratin results in which of the following?
(Multiple Choice)
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A protein with five disulfide bonds was treated with -mercaptoethanol and urea. Once the protein was denatured, the -mercaptoethanol and urea were removed by dialysis. What is the likelihood that all five disulfide bonds will reform correctly?
(Multiple Choice)
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Show the most likely interaction that would occur between a serine residue and a glutamine residue.
(Essay)
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If two protein subunits produced the following structure, what term would be used to describe the interactions that hold the two peptides together? 

(Multiple Choice)
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In a typical Ramachandran plot, _____ is plotted vs _____ to illustrate _______.
(Multiple Choice)
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What type of interaction occurs between the -sheets of fibroin?
(Multiple Choice)
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Which of the following contributes to a positive G for protein folding?
(Multiple Choice)
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Which of the following types of secondary structure has a non-integer value of residues per turn?
(Multiple Choice)
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Show the reaction catalyzed by prolyl isomerase. Indicate the configuration of both substrate and product. 

(Essay)
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Which of the following causes denaturation of a protein when disulfide bonds are present?
(Multiple Choice)
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