Exam 4: Protein Structure

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Protein secondary structures such as α\alpha -helices and β\beta -sheets are stabilized mainly by

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Draw the reaction by which a protein disulfide bond forms.

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Which statement about amino acids is true?

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The amino acid with the most hydrophobic side chain is

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All of the following are types of protein secondary structure EXCEPT

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Describe generally how a gain-of-function protein folding disease can lead to cell death.

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Shown is the titration curve for the amino acid aspartic acid. Draw the predominant protonation state of aspartic acid found at point A in the curve. Shown is the titration curve for the amino acid aspartic acid. Draw the predominant protonation state of aspartic acid found at point A in the curve.

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Would a nonsense mutation in a gene encoding a protein be expected to result in a gain-of-function or a loss-of-function protein folding disease?

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How many possible unique triplet codons could there be in a genome?

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Which represents the correct arrangement of bonding in a peptide bond?

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List the levels of protein structure and give a brief description of each.

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Which of the following statements about the chamber-type chaperone protein GroEL-GroES is correct?

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The dipole moment associated with a peptide bond proceeds from which amide?

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The protein fold known as the Rossman fold is found in proteins that commonly bind

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Which statement about the α\alpha -helix is true?

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Which amino acid side chain from the list below is the most polar?

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Which gives rise to a favorable enthalpic ( Δ\Delta S) driving force for protein folding?

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What is the approximate net charge of the molecule shown below at pH 7? What is the approximate net charge of the molecule shown below at pH 7?

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Cells deal with misfolded proteins by

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How many possible protein primary structures are there for a tripeptide given the 20 amino acids?

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