Exam 6: The Three-Dimensional Structure of Proteins

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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?

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D

Which of the following structural proteins is correctly paired with the modified amino acid or cross-link that is an integral part of that protein?

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A

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?

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B

The presence of a hydrophobic amino acid at every third or fourth residue in α\alpha -keratin results in which of the following?

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What type of interaction occurs between the β\beta -sheets of fibroin?

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Show the reaction catalyzed by prolyl isomerase.Indicate the configuration of both substrate and product. Show the reaction catalyzed by prolyl isomerase.Indicate the configuration of both substrate and product.

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In a typical Ramachandran plot,_____ is plotted vs _____ to illustrate _______.

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Which of the following could contribute to quaternary structure?

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Show the most likely interaction that would occur between a serine residue and a glutamine residue.

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Draw a section of antiparallel β\beta -sheet showing two sheets with three residues in each sheet.Clearly show the hydrogen bond pattern between the two sheets.

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Which of the following causes denaturation of a protein when disulfide bonds are present?

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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?

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Which of the following types of secondary structure has a non-integer value of residues per turn?

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A protein with five disulfide bonds was treated with β\beta -mercaptoethanol and urea.Once the protein was denatured,the β\beta -mercaptoethanol and urea were removed by dialysis.What is the likelihood that all five disulfide bonds will reform correctly?

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Which of the following correctly defines the angles Φ\varPhi and Ψ\varPsi ?

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Which amino acid is often referred to as a "helix-breaker" due to its absence from α\alpha -helices but is often found in structures such as β\beta -turns?

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Which of the following contributes to a positive Δ\Delta G for protein folding?

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Which of the following is true regarding β\beta -sheet structures?

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If a peptide was composed entirely of α\alpha -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?

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The two amino acids most often found in a polyproline II helix are proline and _______.

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