Biochemistry-8th-Edition-Berg-Test-Bank.pdf - Biochemistry...

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Unformatted text preview: Biochemistry 8th Edition Berg Test Bank Full clear download (no error formatting) at : Chapter 2 Protein Composition and Structure 1) Which of the following is most often found in proteins? A) B) C) D) E) D-amino acids L-amino acids an equal amount of D- and L-amino acids amino acids with the -carbon exclusively having an R absolute configuration amino acids with the -carbon exclusively having an S absolute configuration Answer: B Section: 2.1 2) A term that describes a molecule that contains both positive and negative charges but overall has a neutral charge is _. A) B) C) D) E) enantiomer amino acid racemate zwitterion amphipath Answer: D Section: 2.1 3) Which amino acid forms disulfide bonds? A) B) C) D) E) histidine methionine proline serine cysteine Answer: E Section: 2.1 4) pH? Which of the following amino acids has an ionizable R-group with a pKa near neutral A) B) C) D) E) histidine serine aspartic acid lysine tyrosine Answer: A Section: 2.1 5) Formation of a peptide bond produces A) B) C) D) E) ammonia carbon dioxide water H+ OH– as a byproduct. Answer: C Section: 2.2 6) What type of plot allows one to investigate the likely phi and psi angles of the peptide backbone? A) B) C) D) E) Hill Lineweaver-Burk Hanes-Woolf Ramachandran Michaelis-Menten Answer: D Section: 2.2 7) What level of protein structure is composed of helices, sheets, and turns? A) B) C) D) E) primary secondary tertiary quaternary both secondary and tertiary Answer: B Section: 2.3 8) The overall three-dimensional structure of a single polypeptide is referred to as A) B) C) D) E) primary structure secondary structure tertiary structure quaternary structure both secondary structure and tertiary structure _. Answer: C Section: 2.4 Fill-in-the-Blank Questions 9) Ans: -Keratin is a fibrous protein and is the primary component of wool and hair. Section: 2.3 10) Every third residue in the protein collagen is Ans: glycine Section: 2.3 . 11) Disulfide bonds in proteins can be reduced to free sulfhydryl groups by reagents such as . Ans: β-mercaptoethanol Section: 2.6 12) A protein is considered to be coiled structure without its normal activity. Ans: denatured Section: 2.6 when it is converted into a randomly 13) cartilage, and teeth. Ans: Collagen Section: 2.3 is the major fibrous protein present in skin, bone, tendon, 14) Collagen contains Ans: hydroxyproline Section: 2.3 _, a modified amino acid. 15) Agents such as by disrupting the noncovalent interactions. Ans: urea Section: 2.6 and guanidinium chloride denature proteins 16) nature of their interactions. Ans: Quaternary structure refers to the spatial arrangement of subunits and the Section: 2.5 17) The β-sheet structure occurs when the two strands are oriented in the same directions (N → C). Ans: parallel Section: 2.3 Multiple-Choice Questions 18) Which of the following is a function of proteins? A) B) C) D) E) energy carrying molecules catalysts storage of genetic information None of the answers is correct. All of the answers are correct. Ans: B Section: Introduction 19) Key properties of proteins include A) a wide range of functional groups. B) an ability to possess either rigid or flexible structures as dictated by functional requirements. C) the ability to interact with other proteins. D) E) All of the answers are correct. a wide range of functional groups and an ability to possess either rigid or flexible structures as dictated by functional requirements. Ans: D Section: Introduction 20) What is the charged group(s) present in glycine at a pH of 7? A) –NH3+ B) –COO– C) –NH2+ D) –NH3+ and –COO– E) All the charged groups are present. Ans: D Section: 2.1 21) At a pH of 12, what is the charged group(s) present in glycine? A) –NH3+ B) –COO– C) –NH2+ D) –NH3+ and –COO– E) All the charged groups are present. Ans: B Section: 2.1 22) What do the amino acids Tyr, Asn, and Thr have in common? A) B) C) D) E) aromatic rings negatively charged at pH 7.0 positively charged at pH 7.0 double bonds in side chains polar Ans: E Section 2.1 23) Which two amino acids contain a sulfur atom? A) B) C) D) E) serine and methionine serine and threonine methionine and threonine cysteine and methionine cysteine and threonine Ans: D Section: 2.1 24) Which of the following pairs of amino acids is positively charged at a neutral pH? A) B) C) D) E) Lys, Arg Tyr, Arg Cys, Met Leu, Pro Asp, Glu Ans: A Section: 2.1 25) In the following peptide, which amino acid is the N-terminus? Phe-Ala-Gly-Arg A) Phe B) Ala C) Gly D) Arg E) Phe and Arg Ans: A Section: 2.2 26) What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.) A) 2,000 B) 11,000 C) 22,000 D) 222,000 E) None of the answers is correct. Ans: C Section: 2.2 27) Which individual won a Nobel Prize for his (her) landmark work in sequencing the protein insulin? A) Pauling B) McClintock C) Gilbert D) Maxam E) Sanger Ans: E Section: 2.2 28) Why is the peptide bond planar? A) B) C) D) E) Bulky side chains prevent free rotation around the bond. It contains partial double-bond character, preventing rotation. Hydrogen bonding between the NH and C=O groups limits movement. All of the answers are correct. None of the answers is correct. Ans: B Section: 2.2 29) The configuration of most peptide bonds in a protein is _. A) cis B) circular C) parallel D) trans E) perpendicular Ans: D Section: 2.2 30) What structure(s) did Pauling and Corey predict in 1951? A) α helix B) β sheet C) β turns D) Pauling and Corey predicted all three of these structures. E) α helix and β sheet Ans: E Section: 2.4 31) The term “quaternary” with respect to protein structure means A) a repeating structure stabilized by intrachain hydrogen bonds. B) the ability to form all four kinds of noncovalent bonds. C) a multisubunit structure. D) a linear sequence of four amino acids. E) None of the answers is correct. Ans: C Section: 2.5 32) Where are Ω and β turns and loops often found? A) B) C) D) in a hydrophobic pocket on the interior cleft at the protein interface with ligand on the surface of proteins E) None of the answers is correct. Ans: D Section: 2.3 33) What are some of the modifications that proteins acquire? A) B) C) D) E) cleavage and trimming of the protein addition of carbohydrate groups phosphorylation of certain groups All of these are modifications proteins acquire. addition of carbohydrate groups and phosphorylation of certain groups Ans: D Section: 2.6 34) Which of the following amino acid residues would most likely be buried in the interior of a water-soluble, globular protein? A) B) C) D) E) Asp Ser Phe Lys Gln Ans: C Section 2.5 Short-Answer Questions 35) How does a protein’s amino acid sequence influence the tertiary structure? Ans: A protein will spontaneously fold into a three-dimensional structure determined by the amino acid sequence. Section: Introduction 36) What is the advantage of having 20 different amino acids available to form proteins? Ans: The amino acids provide a rich diversity of functional groups, which can independently contribute to protein structure and function. In addition, many can be modified, increasing the diversity of functional groups. Section: Introduction 37) What is the advantage of protein interaction and assembly with other proteins? Ans: When proteins interact or assemble, new functions and specificity become available. Protein interactions allow new binding sites at the assembly interface, as well as providing multifunctional activity and specificity, such as found in polymerases and signal transduction. Section: Introduction 38) What are the three aromatic amino acids? Ans: phenylalanine, tyrosine, and tryptophan Section: 2.1 39) Which amino acid side chains are capable of ionization? Ans: The amino acids are Asp, Glu, His, Cys, Tyr, Lys, and Arg. Section: 2.1 40) How does the protein backbone add to structural stability? Ans: The protein backbone contains the peptide bond, which is an amide containing an NH group and a C=O (carbonyl) group. Peptide bonds are kinetically stable once formed, having very low rates of hydrolysis. Hydrogen-bond formation between the hydrogen on the nitrogen and the oxygen from other carbonyls in either alpha helices or in beta sheets support the protein conformation. Section: 2.2 41) Why are all the theoretical combinations of phi and psi not possible? Ans: Steric hindrances of the side chains make certain combinations and angles impossible. Section: 2.2 42) Describe some of the features of an α helix. Ans: 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. Section: 2.3 43) What is the “hydrophobic effect” as it relates to protein structure? Ans: The three-dimensional structure of a water-soluble protein is stabilized by the tendency of hydrophobic groups to assemble in the interior of the molecule. Section: 2.1 44) -Keratin is referred to as a coiled-coil protein. Describe the protein structure of keratin. Ans: Two α helices entwined to form a very stable double helix of approximately 100 nm in length. Section: 2.3 45) What are prions? Ans: Prions are proteins that can assume (after infection or by other causes) a new protein structure, which is self-propagating. Mammalian prion diseases are fatal. Section: 2.6 46) What does the modification involving the attachment of acetyl groups to the amino termini of proteins do? Ans: The acetylation of the amino termini of proteins makes these proteins more resistant to degradation. Section: 2.6 47) In the ribonuclease experiments performed by Anfinsen, what was the significance of the presence of the reducing agent β-mercaptoethanol? Ans: The reducing agent reduced incorrectly paired disulfide bonds, allowing them to reform with the correct pairing until the most stable conformation of the protein had been obtained. Section: 2.6 48) What is the advantage of having certain areas of partially correct folded regions? Ans: If some regions interact preferentially, lending stability to certain conformations as the protein folds, they can impact the overall structure of the protein. Section: 2.6 Biochemistry 8th Edition Berg Test Bank Full clear download (no error formatting) at : biochemistry 8th edition berg pdf biochemistry berg 7th edition biochemistry (8th edition) pdf biochemistry berg 7th edition pdf stryer biochemistry 9th edition biochemistry 8th edition berg ebook 9781464126109 pdf berg tymoczko stryer biochemistry 6th edition pdf ...
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