Exam 4: Protein Structure
Exam 1: Principles of Biochemistry100 Questions
Exam 2: Physical Biochemistry: Energy Conversion, Water, and Membranes100 Questions
Exam 3: Nucleic Acid Structure and Function100 Questions
Exam 4: Protein Structure100 Questions
Exam 5: Methods in Protein Biochemistry100 Questions
Exam 6: Protein Function114 Questions
Exam 7: Enzyme Mechanisms106 Questions
Exam 8: Cell Signaling Systems102 Questions
Exam 9: Glycolysis: a Paradigm of Metabolic Regulation100 Questions
Exam 10: The Citrate Cycle100 Questions
Exam 11: Oxidative Phosphorylation99 Questions
Exam 12: Photosynthesis100 Questions
Exam 13: Carbohydrate Structure and Function100 Questions
Exam 14: Carbohydrate Metabolism100 Questions
Exam 15: Lipid Structure and Function100 Questions
Exam 16: Lipid Metabolism100 Questions
Exam 17: Amino Acid Metabolism100 Questions
Exam 18: Nucleotide Metabolism99 Questions
Exam 19: Metabolic Integration101 Questions
Exam 20: DNA Replication, Repair, and Recombination99 Questions
Exam 21: RNA Synthesis, Processing, and Gene Silencing100 Questions
Exam 22: Protein Synthesis, Posttranslational Modification, and Transport100 Questions
Exam 23: Gene Regulation100 Questions
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Protein secondary structures such as -helices and -sheets are stabilized mainly by
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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.


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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 amino acid side chain from the list below is the most polar?
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Which gives rise to a favorable enthalpic ( S) driving force for protein folding?
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What is the approximate net charge of the molecule shown below at pH 7? 

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