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Multiple Choice Questions
1. Chemical foundations Page: 14 Difficulty: 1 Ans: B What functional groups are present on this molecule?
A) ether and aldehyde B) hydroxyl and aldehyde C) hydroxyl and carboxylic acid D) hydroxyl and ester E) hydroxyl and ketone 2. Chemical foundations Page: 17 Difficulty: 1 Ans: D Stereoisomers that are nonsuperimposable mirror images of each other are known as: A) anomers. B) cis-trans isomers. C) diastereoisomers. D) enantiomers. E) geometric isomers. 3. Physical foundations Page: 23 Difficulty: 1 Ans: C If heat energy is absorbed by the system during a chemical reaction, the reaction is said to be: A) at equilibrium. B) endergonic. C) endothermic. D) exergonic. E) exothermic. 4. Physical foundations Page: 23 Difficulty: 2 Ans: D If the free energy change ∆ G for a reaction is -46.11 kJ/mol, the reaction is: A) at equilibrium. B) endergonic. C) endothermic. D) exergonic. E) exothermic. 5. Physical foundations Page: 26 Difficulty: 2
C) increasing the activation energy. 20 Difficulty: 3 Differentiate between configuration and conformation. Ans: Configuration denotes the spatial arrangement of the atoms of a molecule that is conferred by . hydrophobic interaction with lipids that provide a folding framework. bonds? Ans: (a) Noncovalent interactions include hydrogen bonds. Thus a molecule with one chiral carbon will have two stereoisomers. which may be distinguishable from one another in a biological system. Chemical foundations Pages: 17. (b) Why is it important that these interactions be noncovalent. and cannot be superimposed on its mirror image—as a right hand cannot fit into a left glove. (b) Because noncovalent interactions are weak. 7. how many amino acids are in the protein. D) catabolic. Cellular foundations Page: 11 Difficulty: 2 (a) List the types of noncovalent interactions that are important in providing stability to the threedimensional structures of macromolecules. rather than covalent. Short Answer Questions 8. and hydrophobic interactions. 10. ionic interactions between charged groups. 9. Physical foundations Page: 27 Difficulty: 1 Ans: B Energy requiring metabolic pathways that yield complex molecules from simpler precursors are: A) A) amphibolic. 6. D) increasing the amount of free energy released. break. E) increasing the energy of the transition state. Chemical Foundations Pages: 17-18 Difficulty: 2 Why is an asymmetric carbon atom called a chiral center? Ans: An asymmetric carbon has four different substituents attached. they can form. modification during interactions with ribosomes. van der Waals interactions. the sequence of amino acids in the protein. E) heterotrophic. and re-form more rapidly and with less energy input than can covalent bonds. This is important to maintain the flexibility needed in macromolecules. Genetic foundations Page: 30 Difficulty: 2 Ans: E The three-dimensional structure of a protein is determined primarily by: A) B) C) D) E) electrostatic guidance from nucleic acid structure. B) anabolic. C) autotrophic. B) decreasing the amount of free energy released.2 Chapter 1 The Foundations of Biochemistry Enzymes are biological catalysts that enhance the rate of a reaction by: decreasing the activation energy.
Configurational isomers can only be interconverted by temporarily breaking covalent bonds.Chapter 1 The Foundations of Biochemistry 3 the presence of either double bonds. 11. without breaking any bonds. are free to assume different positions in space because of the freedom of bond rotation. but mirror images of each other. he was able to separate the two types of crystals found in tartaric acid (racemic acid) that are identical in shape. One may be beneficial. Physical foundations Pages: 26-27 Difficulty: 2 (a) On the reaction coordinate diagram shown below. or one enantiomer may be ineffective and its presence could reduce the efficacy of the other enantiomer. the other toxic. How. do cells accomplish this process? Ans: The endergonic (thermodynamically unfavorable) reaction is coupled to an exergonic (thermodynamically favorable) reaction through a shared intermediate. . or chiral centers. Chemical foundations Pages: 17. One sample rotated polarized light to the left. so each of the two enantiomers of the drug may have very different effects on an organism. 12. around which there is no freedom of rotation. label the transition state and the overall freeenergy change (∆ G) for the uncatalyzed reaction A → B. which give rise to stereoisomers. (b) Is this an exergonic or endergonic reaction? (c) Draw a second curve showing the energetics of the reaction if it were enzymecatalyzed. Why is it important that she separate the two enantiomers and test each for its biological activity? Ans: Biomolecules such as receptors for drugs are stereospecific. Conformation refers to the spatial arrangement of substituent groups that. then. the mirror image crystals rotated polarized light to the right. Chemical foundations Pages: 20-21 Difficulty: 3 A chemist working in a pharmaceutical lab synthesized a new drug as a racemic mixture. (b) Using fine forceps. 13. 14. Physical foundations Page: 23 Difficulty: 2 The free-energy change for the formation of a protein from the individual amino acids is positive and is thus an endergonic reaction. 19 Difficulty: 3 (a) What is optical activity? (b) How did Louis Pasteur arrive at an explanation for the phenomenon of optical activity? Ans: (a) Optical activity is the capacity of a substance to rotate the plane of plane-polarized light. so that the overall free-energy change of the coupled reactions is negative (the overall reaction is exergonic).
B) In liquid water. C) membrane structure. 5.) (b) exergonic reaction Chapter 2 Water Multiple Choice Questions 1. E) primarily involve the effect of polar solutes on the entropy of aqueous systems. E) all of the above are true. B) is a hydrated hydrogen ion. Weak interactions in aqueous systems Page: 53–54 Difficulty: 2 Ans: E Hydrophobic interactions make important energetic contributions to: A) binding of a hormone to its receptor protein. B) enzyme-substrate interactions. 3. 1-27. C) Individual hydrogen bonds are much weaker than covalent bonds. weak acids. C) is a hydrated proton. Weak interactions in aqueous systems Page: 47–49 Difficulty: 2 Ans: D Which of these statements about hydrogen bonds is not true? A) Hydrogen bonds account for the anomalously high boiling point of water. and weak bases Page: 60 Difficulty: 2 Ans: E A hydronium ion: A) has the structure H3O+. Ionization of water. 4. D) involve the ability of water to denature proteins. D) Individual hydrogen bonds in liquid water exist for many seconds and sometimes for minutes. B) do not contribute to the structure of water-soluble proteins. E) The strength of a hydrogen bond depends on the linearity of the three atoms involved in the bond. p. and weak bases Page: 61 Difficulty: 2 Ans: A The pH of a solution of 1 M HCl is: . Ionization of water. the average water molecule forms hydrogen bonds with three to four other water molecules. weak acids. C) have bonding energies of approximately 20–40 Kjoule per mole. 2. Weak interactions in aqueous systems Page: 53 Difficulty: 2 Ans: A A true statement about hydrophobic interactions is that they: A) are the driving force in the formation of micelles of amphipathic compounds in water.4 Chapter 1 The Foundations of Biochemistry Ans: (a) and (c) (See Fig. D) is the usual form of one of the dissociation products of water in solution. E) all of the above are true. 27. D) three-dimensional folding of a polypeptide chain.
The ionic form that predominates at pH 3. Ionization of water.189 times the [H+] as the gastric juice.75). E) none of the above. while gastric juice is pH 1.000 times lower [H+] than the gastric juice. and weak bases Page: 63 Difficulty: 1 Ans: D The aqueous solution with the lowest pH is: A) 0. and weak bases Page: 63 Difficulty: 2 Ans: B Phosphoric acid is tribasic. E) 10–12 M NaOH. and weak bases Page: 62 Difficulty: 2 Ans: D Which of the following is true about the properties of aqueous solutions? A) A pH change from 5. 10. The blood sample has: A) 0. 7. 9.1 C) 1 D) 10 E) –1 6.1 M HCl. 8.0 reflects a decrease in the proton concentration ([H+]) by a factor of 100. the salt concentration is higher than that of the acid. C) HPO42–. with pKa’s of 2. D) 0. C) 0. B) A pH change from 8.4. D) PO43–. weak acids. weak acids.86). B) 5. E) a million times lower [H+] than the gastric juice. At pH values lower than the pKa.0 reflects an increase in the hydroxide ion concentration ([OH-]) of 20%.29 times lower [H+] than the gastric juice.14. C) 6 times lower [H+] than the gastric juice. weak acids. C) Charged molecules are generally insoluble in water.4.0 to 6. E) The pH can be calculated by adding 7 to the value of the pOH. B) H2PO4–.2 is: A) H3PO4. 6.0 to 6. .Chapter 1 The Foundations of Biochemistry 5 A) 0 B) 0. weak acids.1 M acetic acid (pKa = 4. Buffering against pH changes in biological systems Page: 65–66 A) B) Difficulty: 2 Ans: E Which of the following statements about buffers is true? A buffer composed of a weak acid of pKa = 5 is stronger at pH 4 than at pH 6.1 M formic acid (pKa = 3.01 M HCl.4. D) Hydrogen bonds form readily in aqueous solutions.86. and 12. Ionization of water. Ionization of water. Ionization of water. and weak bases Page: 62 Difficulty: 2 Ans: E The pH of a sample of blood is 7. B) 0. D) 6.
4 E) 7. 14. the: A) pH remains constant.8 C) 7. B) does not explain the behavior of di.0 M hydrochloric acid. D) The strongest buffers are those composed of strong acids and strong bases. C) pH rises more than if an equal amount of NaOH is added to unbuffered water at pH 4.5 B) 6. E) relates the pH of a solution to the pKa and the concentrations of acid and conjugate base. 11.76.4.or tri-basic weak acids C) employs the same value for pKa for all weak acids. B) pH rises more than if an equal amount of NaOH is added to an acetate buffer initially at pH 6. .76). The resulting solution is pH: A) 6.5 12. D) is equally useful with solutions of acetic acid and of hydrochloric acid. Buffering against pH changes in biological systems Page: 65–67 Difficulty: 3 Ans: D A compound has a pKa of 7. 13.0 is added 30 mL of 1. When sodium hydroxide (NaOH) is mixed with this buffer. Buffering against pH changes in biological systems Page: 66-67 Difficulty: 2 Ans: E The Henderson-Hasselbalch equation: A) allows the graphic determination of the molecular weight of a weak acid from its pH alone. the weak acid and salt concentrations in a buffer are equal. initially at the same pH as its pKa (4. Buffering against pH changes in biological systems Page: 66–67 Difficulty: 2 Ans: C 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. D) ratio of acetic acid to sodium acetate in the buffer falls. Buffering against pH changes in biological systems Page: 66–67 Difficulty: 2 Ans: D Consider an acetate buffer. E) When pH = pKa. To 100 mL of a 1. 1 M acetic acid 1 M sodium acetate Buffer 1: 10 mL 90 mL Buffer 2: 50 mL 50 mL Buffer 3: 90 mL 10 mL Which of these statements is true of the resulting buffers? A) B) C) D) pH of buffer 1 < pH of buffer 2 < pH of buffer 3 pH of buffer 1 = pH of buffer 2 = pH of buffer 3 pH of buffer 1 > pH of buffer 2 > pH of buffer 3 The problem cannot be solved without knowing the value of pKa.6 Chapter 1 The Foundations of Biochemistry C) The pH of a buffered solution remains constant no matter how much acid or base is added to the solution.0 M solution of this compound at pH 8. E) sodium acetate formed precipitates because it is less soluble than acetic acid.76.2 D) 7.
14 H2PO4– HPO42– 6. weak acids. and the second (pKa = 6. The dominant form at pH 4 is therefore H2PO4–. RNH2. and weak bases Page: 63 Difficulty: 2 Phosphoric acid (H3PO4) has three dissociable protons. (2) electrostatic interactions: relatively weak charge-charge interactions (attractions of opposite charges.Chapter 1 The Foundations of Biochemistry 7 E) None of the above. circle the conjugate base. weak acids. Ionization of water. repulsions of like charges) between two ionized groups.14) has been titrated completely. which occurs when the weak acid has been exactly one half titrated with NaOH. Buffering against pH changes in biological systems Page: 64–66 Difficulty: 2 Give the general Henderson-Hasselbalch equation and sketch the plot it describes (pH against amount of NaOH added to a weak acid). The region of greatest buffering capacity . occurs at a pH equal to the pKa of the weak acid.86 12. the form with one dissociated proton (see Fig. H2PO4–.86) has just started to be titrated. Short Answer Questions 15. 18. Weak interactions in aqueous systems Page: 47–55 Difficulty: 2 Name and briefly define four types of noncovalent interactions that occur between biological molecules. RCOOH RNH2 H2PO4– H2CO3 RCOO– RNH3+ H3PO4 HCO3– Ans: RCOO–. Ionization of water. (3) hydrophobic interactions: the forces that tend to bring two hydrophobic groups together. Which form of phosphoric acid predominates in a solution at pH 4? Explain your answer. (4) van der Waals interactions: weak interactions between the electric dipoles that two close-spaced atoms induce in each other. and indicate the region in which the buffering capacity of the system is greatest. 2-16). On your curve label the pKa for the weak acid. HCO3– 17. 16. reducing the total area of the two groups that is exposed to surrounding molecules of the polar solvent (water). Ans: (1) Hydrogen bonds: weak electrostatic attractions between one electronegative atom (such as oxygen or nitrogen) and a hydrogen atom covalently linked to a second electronegative atom.4 Ans: At pH 4. Acid pKa H3PO4 2. the first dissociable proton (pKa = 2. Ans: The inflection point. with the pKa’s shown below. and weak bases Page: 63 Difficulty: 1 For each of the pairs below.
What is the pH at this point? Ans: The plot of pH vs. show how you would calculate the ratio of acid to salt at pH 5.2. p. HA.68 20.5 mM) completely titrates the acid so that it can no longer act as a buffer and leaves 150 mmol of .8 Chapter 1 The Foundations of Biochemistry (where the titration curve is flattest) occurs at pH values of pKa ±1.22 22.48 = 3.7 + log (0. 65. Buffering against pH changes in biological systems Page: 65 Difficulty: 3 Draw the titration curve for a weak acid. the pH at this point can be calculated: pH = pKa + log [ o j gt c nu ae [ cd ai ] bs ] ae = 3.1 M sodium acetate? Ans: pH = pKa + log [ o j gt c nu ae [ cd ai ] bs ] ae = 4.1/0. Label the axes properly.7 + log (5/150) = 4.7) and 0.7). What is the pH of the resulting solution? Ans: pH = pKa + log [ o j gt c nu ae [ cd ai ] bs ] ae = 4.2 + log 3 = 3.2) = 4.5 M NaOH.5 M) to 50 mmol of acetic acid (100 mL × 0.5 mol of acetic acid per liter to 400 mL of 0. p. Buffering against pH changes in biological systems Page: 66–67 Difficulty: 2 You have just made a solution by combining 50 mL of a 0. From the Henderson-Hasselbalch equation.7 – 1. Ans: 23.2 M acetic acid (pKa = 4.) 19. whose pKa is 3. added base should have the general shape of those shown in Fig. 2-18.2 + 0.7 – 0.3 = 4.4 21.1 M sodium acetate solution with 150 mL of 1 M acetic acid (pKa = 4. with the midpoint of the titration (inflection point) at pH 3. Buffering against pH changes in biological systems Page: 66–67 Difficulty: 2 For a weak acid with a pKa of 6. The ratio of A– to HA is 3 when 0. 2-18.7. What is the final pH? (The pKa of acetic acid is 4.75 equivalents of base have been added.48 = 3. Buffering against pH changes in biological systems Page: 66-67 Difficulty: 3 Suppose you have just added 100 mL of a solution containing 0.) Ans: Addition of 200 mmol of NaOH (400 mL × 0. Buffering against pH changes in biological systems Page: 66–67 Difficulty: 2 What is the pH of a solution containing 0.0. (See Fig. Indicate with an arrow where on the curve the ratio of salt (A–) to acid (HA) is 3:1.2. 65.
by definition. Amino acids Page: 79 Difficulty: 1 Ans: A All of the amino acids that are found in proteins. D) is in the L absolute configuration in naturally occurring proteins. Buffering against pH changes in biological systems Page: 66-67 Difficulty: 2 A weak acid HA.Chapter 1 The Foundations of Biochemistry 9 NaOH dissolved in 500 mL. pH = pKa + log [ o j gt c nu ae [ cd ai ] bs ] ae = 5.3 M. what would the final pH be? Ans: Combining 1 mol of weak acid with 0.1/0. an [OH–] of 0.9) = 4. If 1.9 mol of weak acid and 0.0 mol of this acid and 0. Amino acids Page: 76 Difficulty: 2 Ans: B Of the 20 standard amino acids.48. [H+] can be calculated from the water constant: [H+][OH–] = 10–14 [H+] = 10–14 M2 / 0. log (1/[H+]) pH = log (0. 24. is unbranched D) lysine. E) is symmetric. except for proline. is a simple methyl group B) glycine.0.1 mol of salt.1 mol of NaOH were dissolved in one liter of water. and Proteins Multiple Choice Questions 1. is a carboxylic acid. Given [OH–].1 mol of NaOH yields 0.3 M /10–14 M2) = 12. A) B) . has a pKa of 5. 2. contain a(n): A) amino group. only ___________ is not optically active. forms a covalent bond with the amino group 3. The reason is that its side chain ___________. is a hydrogen atom C) glycine. contains only nitrogen E) proline. B) carbonyl group. Peptides.3 M pH is. Amino acids Page: 76 Difficulty: 1 Ans: C The chirality of an amino acid results from the fact that its α carbon: has no net charge. A) alanine.0 + log (0. C) is bonded to four different chemical groups.05 Chapter 3 Amino Acids.
8. C) Cystine is formed by the oxidation of the carboxylic acid group on cysteine. derived by linking two standard amino acids. tryptophan absorbs more ultraviolet light than tyrosine. − B) —COOH + —NH2 → —COO + —NH2+. B) Histidine’s ring structure results in its being categorized as aromatic or basic. at any pH below the pI of the amino acid. D) ester group. Amino acids Page: 81 Difficulty: 1 Ans: A Amino acids are ampholytes because they can function as either a(n): A) A) acid or a base. Amino acids Page: 84 Difficulty: 2 Ans: B For amino acids with neutral R groups. depending on pH. E) thiol group. C) On a molar basis.10 Chapter 1 The Foundations of Biochemistry C) carboxyl group. The titration reaction occurring at pK2 (pK2 = 9. Amino acids Page: 80 Difficulty: 2 Ans: A Which of the following statements about cystine is correct? Cystine forms when the —CH2—SH R group is oxidized to form a —CH2—S—S—CH2 — disulfide bridge between two cysteines. C) polar or a nonpolar molecule. − − E) —NH2 + OH → —NH + H2O. E) transparent or a light-absorbing compound. D) Cystine is formed through a peptide linkage between two cysteines. Amino acids Pages: 82–83 Difficulty: 2 Ans: D Titration of valine by a strong base. 7. B) neutral molecule or an ion. for example NaOH. D) standard or a nonstandard monomer in proteins. D) The major contribution to the characteristic absorption of light at 280 nm by proteins is the phenylalanine R group. E) The presence of a ring structure in its R group determines whether or not an amino acid is aromatic. B) Cystine is an example of a nonstandard amino acid. reveals two pK’s. − + D) —NH3 + OH → —NH2 + H2O. 6. 5. Amino acids Pages: 79–80 Difficulty: 3 Ans: C Which of the following statements about aromatic amino acids is correct? A) All are strongly hydrophilic. 4. E) Two cystines are released when a —CH2—S—S—CH2— disulfide bridge is reduced to —CH2—SH.62) is: A) —COOH + OH → —COO + H2O. − C) —COO + —NH2+ → —COOH + —NH2. the population of amino acids in solution will have: − − .
000 amino acids. 9. E) two free carboxyl groups. C) The number 110 reflects the number of amino acids found in the typical small protein. C) one free amino group on a glycyl residue and one free carboxyl group on an alanyl residue. Peptides and proteins Page: 86 Difficulty: 1 Ans: C An octapeptide composed of four repeating glycylalanyl units has: A) one free amino group on an alanyl residue. as well as the loss of water when the peptide bond forms. E) positive and negative charges in equal concentration. D) The number 110 takes into account the relatively small size of nonstandard amino acids. 11. B) one free amino group on an alanyl residue and one free carboxyl group on a glycyl residue. Why? A) The number 110 is based on the fact that the average molecular weight of a protein is 110. 12. B) a net positive charge. Peptides and proteins Page: 87 Difficulty: 2 Ans: B The average molecular weight of the 20 standard amino acids is 138. and only small proteins have their molecular weight estimated this way. C) no charged groups. E) two free amino groups. both on glycyl residues. Peptides and proteins . B) The number 110 reflects the higher proportion of small amino acids in proteins. D) two free amino and two free carboxyl groups. D) no free carboxyl group. C) four peptide bonds. Peptides and proteins Page: 86 Difficulty: 1 Ans: C The peptide alanylglutamylglycylalanylleucine has: A) a disulfide bridge. 10.Chapter 1 The Foundations of Biochemistry 11 A) a net negative charge. E) The number 138 represents the molecular weight of conjugated amino acids. B) five peptide bonds. but biochemists use 110 when estimating the number of amino acids in a protein of known molecular weight.000 with an average of 1. D) no net charge. Peptides and proteins Page: 88 Difficulty: 1 Ans: B Which of the following refers to particularly stable arrangements of amino acid residues in a protein that give rise to recurring patterns? A) Primary structure B) Secondary structure C) Tertiary structure D) Quaternary structure E) None of the above 13.
3-5. (3) aromatic. (2) polar. (See Fig. p. Amino acids Page: 79 Difficulty: 1 Only one of the common amino acids has no free α -amino group. 3-5. uncharged. (e) C 17. (5) negatively charged. Amino acids Pages: 78–79 Difficulty: 2 A B C D E __________________________________________________________________ Tyr-Lys-Met Gly-Pro-Arg Asp-Trp-Tyr Asp-His-Glu Leu-Val-Phe Which one of the above tripeptides: ____(a) is most negatively charged at pH 7? ____(b) will yield DNP-tyrosine when reacted with l-fluoro-2. (c) E. 79). Ans: The amino acid L-proline has no free α -amino group. when dissolved in water.12 Chapter 1 The Foundations of Biochemistry Page: 88 Difficulty: 1 Ans: D Which of the following describes the overall three-dimensional folding of a polypeptide? A) B) C) D) E) Primary structure Secondary structure Tertiary structure Quaternary structure None of the above Short Answer Questions 14. Name this amino acid and draw its structure.) 16. (4) positively charged. 79. Ans: Amino acids may be categorized by the chemistry of their R groups: (1) nonpolar aliphatics. but rather has an imino group formed by cyclization of the R-group aliphatic chain with the amino group (see Fig. Amino acids Page: 81 Difficulty: 1 Why do amino acids. the carboxylic acid group (—COOH) will dissociate to become a negatively charged —COO– group.4-dinitrobenzene and hydrolyzed in acid? ____(c) contains the largest number of nonpolar R groups? ____(d) contains sulfur? ____(e) will have the greatest light absorbance at 280 nm? Ans: (a) D. (d) A. Amino acids Pages: 78–79 Difficulty: 2 Briefly describe the five major groupings of amino acids. p. (b) A. and the —NH2 amino group will attract a proton to become a positively . 15. become zwitterions? Ans: Near pH = 7.
or 4[conjugate base] = [acid] Therefore. Amino acids Page: 84 Difficulty: 2 What is the pI.Chapter 1 The Foundations of Biochemistry 13 charged —NH3+ group. . Ans: pH = pKa + log [ o j gt c nu ae [ cd ai ] [acid] [conjugate base] [acid] [conjugate base] [acid] [conjugate base] bs ] ae pKa – pH = log antilog (pKa – pH) = antilog (6.4. Amino acids Page: 84 Difficulty: 2 The amino acid histidine has a side chain for which the pKa is 6.4. at pH 5. the —NH3+ group will be titrated according to the reaction: —NH3+ + OH– → —NH2 + H2O.4) = 4 = [acid]/[conjugate base]. 19. 4/5 (80%) of the histidine will be in the protonated form. Calculate what fraction of the histidine side chains will carry a positive charge at pH 5. pI is the arithmetic mean of a molecule’s two pKa values: pI = 1/2 (pK1 + pK2) 20. what titration reaction will occur around pH = 9. 18. and how is it determined for amino acids that have nonionizable R groups? Ans: The pI is the isoelectric point. or no net charge.5? Ans: Around pH = 9.0. Amino acids Page: 82 Difficulty: 1 As more OH– equivalents (base) are added to an amino acid solution.5. Be sure to show your work.0 – 5. It occurs at a characteristic pH when a molecule has an equal number of positive and negative charges. For amino acids with nonionizable R groups.
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