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1. The enzyme fumarase catalyzes the reversible hydration of fumaric acid to l-malate, but it will not catalyze the hydration of maleic acid, the cis isomer of fumaric acid. This is an example of: A) B) C) D) E) biological activity. chiral activity. racemization. stereoisomerization. stereospecificity.
2. Enzymes are biological catalysts that enhance the rate of a reaction by: A) B) C) D) E) decreasing the activation energy. decreasing the amount of free energy released. increasing the activation energy. increasing the amount of free energy released. increasing the energy of the transition state.
3. Energy requiring metabolic pathways that yield complex molecules from simpler precursors are: A) B) C) D) E) amphibolic. anabolic. autotrophic. catabolic. heterotrophic.
4. Hydrophobic interactions make important energetic contributions to: A) B) C) D) E) binding of a hormone to its receptor protein. enzyme-substrate interactions. membrane structure. three-dimensional folding of a polypeptide chain. all of the above are true.
5. Osmosis is movement of a: A) B) C) D) E) charged solute molecule (ion) across a membrane. gas molecule across a membrane. nonpolar solute molecule across a membrane. polar solute molecule across a membrane. water molecule across a membrane.
8.2 and 9. A 1. A) B) C) D) E) alanine. Which of the following statements about cystine is correct? A) Cystine forms when the —CH2—SH R group is oxidized to form a —CH2—S—S— CH2— disulfide bridge between two cysteines. E) Two cystines are released when a —CH2—S—S—CH2— disulfide bridge is reduced to —CH2—SH. The reason is that its side chain ___________. Of the 20 standard amino acids.0 M solution of a compound with 2 ionizable groups (pKa’s = 6. C) Cystine is formed by the oxidation of the carboxylic acid group on cysteine. only ___________ is not optically active.60 8. 100 mL total) has a pH of 6.0 M HCl to this solution. derived by linking two standard amino acids.13 9. 8. contains only nitrogen proline. is a hydrogen atom glycine. 1 M acetic acid Buffer 1: 10 mL Buffer 2: 50 mL Buffer 3: 90 mL 1 M sodium acetate 90 mL 50 mL 10 mL Which of these statements is true of the resulting buffers? A) pH of buffer 1 < pH of buffer 2 < pH of buffer 3 B) pH of buffer 1 = pH of buffer 2 = pH of buffer 3 C) pH of buffer 1 > pH of buffer 2 > pH of buffer 3 D) The problem cannot be solved without knowing the value of pKa.32 The pH cannot be determined from this information. forms a covalent bond with the amino group 9. 2 . Three buffers are made by combining a 1 M solution of acetic acid with a 1 M solution of sodium acetate in the ratios shown below. the solution will change to pH: A) B) C) D) E) 5. D) Cystine is formed through a peptide linkage between two cysteines.5. If a biochemist adds 60 mL of 1. 7. is a simple methyl group glycine. B) Cystine is an example of a nonstandard amino acid.6. E) None of the above. is unbranched lysine.90 9.
The peptide alanylglutamylglycylalanylleucine has: A) B) C) D) E) a disulfide bridge. four peptide bonds. A) B) C) D) E) cleavage condensation group transfer isomerization oxidation reduction 12. 3 . E) two free carboxyl groups. positive and negative charges in equal concentration.10. both on glycyl residues. no free carboxyl group. 14. lipids. An octapeptide composed of four repeating glycylalanyl units has: A) one free amino group on an alanyl residue. a net positive charge. C) one free amino group on a glycyl residue and one free carboxyl group on an alanyl residue. no net charge. five peptide bonds. 11. The formation of a peptide bond between two amino acids is an example of a(n) ______________ reaction. two free amino groups. no charged groups. metals . Prosthetic groups in the class of proteins known as glycoproteins are composed of: A) B) C) D) E) carbohydrates. phosphates. at any pH below the pI of the amino acid. D) two free amino and two free carboxyl groups. For amino acids with neutral R groups. 13. the population of amino acids in solution will have: A) B) C) D) E) a net negative charge. B) one free amino group on an alanyl residue and one free carboxyl group on a glycyl residue. flavin nucleotides.
In a second step. a strip of this gel is turned 90 degrees. separate proteins exclusively on the basis of molecular weight. placed on another gel containing SDS. 4 .filtration) chromatography? A) B) C) D) E) cytochrome c immunoglobulin G ribonuclease A RNA polymerase serum albumin Mr = 13. preserve a protein’s native structure and biological activity. 18.500 16. it is possible to: A) B) C) D) E) determine a protein’s isoelectric point. The first step in two-dimensional gel electrophoresis generates a series of protein bands by isoelectric focusing. more intense isoelectric focusing. 17.700 Mr = 450. In a mixture of the five proteins listed below. C) the individual bands become visualized by interacting with protein-specific antibodies in the second gel. E) None of the above. occur mainly between electronegative atoms of the R groups. 19.000 Mr = 68. and electric current is again applied. Changing the pH of the elution buffer. A protein retained on an affinity chromatography column is usually eluted off the column by A) B) C) D) Gradually increasing the salt concentration of the elution buffer. determine the amino acid composition of the protein. occur only near the amino and carboxyl termini of the helix. occur only between some of the amino acids of the helix.000 Mr = 13. are roughly perpendicular to the axis of the helix. which should elute second in size-exclusion (gel. Allowing the retained protein to naturally come off the column after the non-specifically bound proteins have first passed through the resin. In this second step: A) proteins with similar isoelectric points become further separated according to their molecular weights. E) the proteins in the bands separate more completely because the second electric current is in the opposite polarity to the first current.000 Mr = 145.15. By adding SDS (sodium dodecyl sulfate) during the electrophoresis of proteins. D) the individual bands undergo a second. B) the individual bands become stained so that the isoelectric focus pattern can be visualized. In the α helix the hydrogen bonds: A) B) C) D) E) are roughly parallel to the axis of the helix. Adding the protein’s free ligand. determine an enzyme’s specific activity.
22.20. α-keratin is a protein in which the polypeptides are mainly in the α-helix conformation. the presence of an Arg residue near the carboxyl terminus of the α helix. two Cys. Amino acid residues commonly found in the middle of β turn are: A) B) C) D) E) Ala and Gly. hydrophobic. those with ionized R-groups. Which of the following statements is false? A) B) C) D) E) Collagen is a protein in which the polypeptides are mainly in the α-helix conformation. Pro and Gly. 23. 5 . interactions between two adjacent hydrophobic Val residues. Silk fibroin is a protein in which the polypeptide is almost entirely in the β conformation. 21. region of steric hindrance determined by the large C=O group. Gly residues are particularly abundant in collagen. region of the peptide bond that contributes to a Ramachandran plot. the plane drawn behind the peptide bond indicates the: A) B) C) D) E) absence of rotation around the C—N bond because of its partial double-bond character. plane of rotation around the Cα—N bond. Disulfide linkages are important for keratin structure. interactions between neighboring Asp and Arg residues. An α helix would be destabilized most by: A) B) C) D) E) an electric dipole spanning several peptide bonds throughout the α helix. theoretical space between –180 and +180 degrees that can be occupied by the φ and ψ angles in the peptide bond. In the diagram below. the presence of two Lys residues near the amino terminus of the α helix.
In the binding of oxygen to myoglobin.24. coherent patterns of folding or function. Some oligomeric proteins can further associate into large fibers. sites. linear with a positive slope. oligomers. All subunits must be identical. The α-keratin chains indicated by the diagram below have undergone one chemical step. 6 . These regions are called: A) B) C) D) E) domains. Some subunits may have nonprotein prosthetic groups. peptides. subunits. Proteins often have regions that show specific. Which of the following statements about oligomeric proteins is false? A) B) C) D) E) A subunit may be similar to other proteins. the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as: A) B) C) D) E) hyperbolic. Many have regulatory roles. sigmoidal. 25. random. To alter the shape of the α-keratin chains—as in hair waving—what subsequent steps are required? A) B) C) D) E) Chemical oxidation and then shape remodeling Chemical reduction and then chemical oxidation Chemical reduction and then shape remodeling Shape remodeling and then chemical oxidation Shape remodeling and then chemical reduction 26. linear with a negative slope. 27.
the transition from T state to R state (low to high affinity) is triggered by: A) B) C) D) E) Fe2+ binding. subunit dissociation. oxygen binding. the weaker the affinity. The amino acid substitution of Val for Glu in Hemoglobin S results in aggregation of the protein because of ___________ interactions between molecules. A) B) C) D) E) covalent disulfide hydrogen bonding hydrophobic ionic 7 . E) two different ligands can bind to the same binding site. The larger the Ka. The Ka is equal to the concentration of ligand when all of the binding sites are occupied. 31. the faster is the binding. In hemoglobin. heme binding. subunit association. It binds with lower affinity to fetal hemoglobin than to adult hemoglobin. 29. 30. The larger the Ka. The Ka is independent of such conditions as salt concentration and pH. Which of the following is not correct concerning 2. It is normally found associated with the hemoglobin extracted from red blood cells. C) binding of the ligand to the protein is covalent. D) multiple molecules of the same ligand can bind to the same binding site. the smaller the Kd (dissociation constant). An allosteric interaction between a ligand and a protein is one in which: A) binding of a molecule to a binding site affects binding of additional molecules to the same site. It increases the affinity of hemoglobin for oxygen. B) binding of a molecule to a binding site affects binding properties of another site on the protein. Which of the following statements about protein-ligand binding is correct? A) B) C) D) E) The larger the Ka (association constant).28. It is an allosteric modulator. 32.3-bisphosphoglycerate (BPG)? A) B) C) D) E) It binds at a distance from the heme groups of hemoglobin.
or “cloned. An individual molecular structure within an antigen to which an individual antibody binds is as a(n): A) B) C) D) E) antigen. A monoclonal antibody differs from a polyclonal antibody in that monoclonal antibodies: A) B) C) D) E) are labeled with chemicals that can be visualized. Fab region.” cells. have only a single polypeptide chain that can recognize an antigen. are synthesized only in living organisms. immunoglobin fragments. macrophage fragments. 35. B cell fragments. Fc region MHC site. are produced by cells from the same organism that produced the antigen. Key 1 2 3 4 5 6 7 8 9 10 E A B E E C A B A B 11 12 13 14 15 16 17 18 19 20 B C C A B E A B A A 21 22 23 24 25 26 27 28 29 30 E C A A D B A E B C 31 32 33 34 35 C D B A C 8 . are synthesized by a population of identical. T cell fragments. 34. epitope.33. The proteins of the Major Histocompatibility Complex (MHC) bind and display: A) B) C) D) E) antigen fragments.
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