Exam 2: Protein Composition and Structure
Exam 1: Biochemistry: an Evolving Science50 Questions
Exam 2: Protein Composition and Structure48 Questions
Exam 3: Exploring Proteins and Proteomes50 Questions
Exam 4: DNA, RNA, and the Flow of Genetic Information50 Questions
Exam 5: Exploring Genes and Genomes50 Questions
Exam 6: Exploring Evolution and Bioinformatics48 Questions
Exam 7: Hemoglobin: a Portrait of a Protein in Action52 Questions
Exam 8: Enzymes: Basic Concepts and Kinetics50 Questions
Exam 18: Oxidative Phosphorylation50 Questions
Exam 9: Catalytic Strategies49 Questions
Exam 10: Regulatory Strategies50 Questions
Exam 11: Carbohydrates50 Questions
Exam 12: Lipids and Cell Membranes49 Questions
Exam 13: Membrane Channels and Pumps51 Questions
Exam 14: Signal-Transduction Pathways49 Questions
Exam 15: Metabolism: Basic Concepts and Design50 Questions
Exam 16: Glycolysis and Gluconeogenesis51 Questions
Exam 17: The Citric Acid Cycle47 Questions
Exam 19: The Light Reactions of Photosynthesis50 Questions
Exam 20: The Calvin Cycle and the Pentose Phosphate Pathway46 Questions
Exam 21: Glycogen Metabolism50 Questions
Exam 22: Fatty Acid Metabolism50 Questions
Exam 23: Protein Turnover and Amino Acid Catabolism49 Questions
Exam 24: The Biosynthesis of Amino Acids48 Questions
Exam 25: Nucleotide Biosynthesis50 Questions
Exam 26: Biosynthesis of Membrane Lipids and Steroids50 Questions
Exam 27: The Integration of Metabolism50 Questions
Exam 28: DNA Replication, Repair, and Recombination48 Questions
Exam 29: Rna Synthesis and Processing47 Questions
Exam 30: Protein Synthesis48 Questions
Exam 31: The Control of Gene Expression in Prokaryotes50 Questions
Exam 32: The Control of Gene Expression in Eukaryotes50 Questions
Exam 33: Sensory Systems49 Questions
Exam 34: The Immune System50 Questions
Exam 35: Molecular Motors50 Questions
Exam 36: Drug Development44 Questions
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Describe some of the features of an α helix.
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The α helix is a coil stabilized by intrachain hydrogen bonds between the carbonyl oxygen of a residue and the amide hydrogen of the fourth residue away. There are 3.6 amino acids per turn. The hydrogen bonds are between amino acid residues that have three intervening residues. Thus, these amino acid residues are found on the same side of the coil. The helix is almost always right-handed, although left-handed helices are, in theory, possible.
What do the amino acids Tyr, Asn, and Thr have in common?
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E
What are some of the modifications that proteins acquire?
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D
What is the charged group(s) present in glycine at a pH of 7?
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In the ribonuclease experiments performed by Anfinsen, what was the significance of the presence of the reducing agent β-mercaptoethanol?
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What does the modification involving the attachment of acetyl groups to the amino termini of proteins do?
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How does a protein's amino acid sequence influence the tertiary structure?
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In the following peptide, which amino acid is the N-terminus?
Phe-Ala-Gly-Arg
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A protein is considered to be __________________ when it is converted into a randomly coiled structure without its normal activity.
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Which of the following amino acids has an ionizable R-group with a pKa near neutral pH?
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What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.)
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_______________ is a fibrous protein and is the primary component of wool and hair.
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What is the advantage of having 20 different amino acids available to form proteins?
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What is the advantage of protein interaction and assembly with other proteins?
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