BIOCHEMISTRY (LL)
9th Edition
ISBN: 9781337805100
Author: Campbell
Publisher: CENGAGE L
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Chapter 9, Problem 57RE
REFLECT AND APPLY Would you expect tRNA or mRNA to be more extensively hydrogen bonded? Why?
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The enzyme lactate dehydrogenase (LDH) catalyzes the conversion of pyruvate to lactatein skeletal muscle cells using NAD/NADH during anaerobic “balanced” fermentation.Answer the following questions about this reaction.
(a) Write out the two reductive half reactions and indicate the E ̊' for each half reaction. Write out the full balanced reaction for the pyruvate to lactate rxn and indicate the ∆E ̊' for the reaction.
(b) What is the free energy change under standard state conditions for thisreaction? Which direction is spontaneous?(c) Assume that in skeletal muscle cells the ratio of [NAD+] to [NADH] is 100, and that the[pyruvate] = 0.40 mM and [lactate] = 4.0 mM. What is the free energy change (∆G')for the conversion of pyruvate to lactate? Indicate the direction in which the reactionis spontaneous under these cellular conditions.
Why did the authors worry about the temperature-dependent solubility of the carriers in thebilayer? How did the authors determine whether the effect of freezing the lipid bilayer wasto decrease the solubility of the carriers (nonactin and valinomycin) or whether the effectwas to impair their ability to diffuse through the membrane (decrease their mobility)?
Kranse et. al. measured the temperature dependence of conductance using membranescontaining the phospholipids glyceryl dipalmitate and glyceryl distearate. Describe themodifications in membrane content that you would employ to:
(a) shift the temperature of the phase transition
(b) make the ion conductance curve for valinomycin andnonactin more like that of gramicidin
Chapter 9 Solutions
BIOCHEMISTRY (LL)
Ch. 9 - REFLECT AND APPLY Consider the following in light...Ch. 9 - Prob. 2RECh. 9 - RECALL What is the structural difference between...Ch. 9 - RECALL Give the name of the base, the...Ch. 9 - RECALL What is the difference between ATP and...Ch. 9 - RECALL Give the sequence on the opposite strand...Ch. 9 - RECALL Are the sequences shown in Question 6 those...Ch. 9 - REFLECT AND APPLY (a) Is it biologically...Ch. 9 - REFLECT AND APPLY A friend tells you that only...Ch. 9 - REFLECT AND APPLY In the early days of molecular...
Ch. 9 - REFLECT AND APPLY Why is RNA more vulnerable to...Ch. 9 - Prob. 12RECh. 9 - RECALL Draw a GC base pair. Draw an AT base pair.Ch. 9 - RECALL Which of the following statements is (are)...Ch. 9 - Prob. 15RECh. 9 - BIOCHEMICAL CONNECTIONS Describe the landmark case...Ch. 9 - Prob. 17RECh. 9 - Prob. 18RECh. 9 - RECALL Which of the following statements is (are)...Ch. 9 - RECALL Define supercoiling, positive supercoil,...Ch. 9 - RECALL What is propeller twist?Ch. 9 - RECALL What is an AG/CT step?Ch. 9 - RECALL Why does propeller-twist occur?Ch. 9 - Prob. 24RECh. 9 - RECALL If circular B-DNA is positively...Ch. 9 - RECALL Briefly describe the structure of...Ch. 9 - Prob. 27RECh. 9 - REFLECT AND APPLY List three mechanisms that relax...Ch. 9 - REFLECT AND APPLY Explain how DNA gyrase works.Ch. 9 - Prob. 30RECh. 9 - REFLECT AND APPLY Would you expect to find...Ch. 9 - REFLECT AND APPLY One of the original structures...Ch. 9 - REFLECT AND APPLY What is the complete base...Ch. 9 - REFLECT AND APPLY Why was it necessary to specify...Ch. 9 - Prob. 35RECh. 9 - Prob. 36RECh. 9 - Prob. 37RECh. 9 - BIOCHEMICAL CONNECTIONS A recent commercial for a...Ch. 9 - REFLECT AND APPLY A technology called PCR is used...Ch. 9 - REFLECT AND APPLY Why does DNA with a high AT...Ch. 9 - RECALL What are the three primary RNA types?Ch. 9 - RECALL What determines the base sequence of all...Ch. 9 - RECALL What is the name of the process that...Ch. 9 - RECALL What is the basic purpose of tRNA?Ch. 9 - RECALL The base sequence of which type of RNA is...Ch. 9 - RECALL What is the name of the process by which...Ch. 9 - Prob. 47RECh. 9 - Prob. 48RECh. 9 - Prob. 49RECh. 9 - RECALL Why do we say that micro RNAs are involved...Ch. 9 - Prob. 51RECh. 9 - Prob. 52RECh. 9 - Prob. 53RECh. 9 - Prob. 54RECh. 9 - Prob. 55RECh. 9 - Prob. 56RECh. 9 - REFLECT AND APPLY Would you expect tRNA or mRNA to...Ch. 9 - REFLECT AND APPLY The structures of tRNAs contain...Ch. 9 - REFLECT AND APPLY Would you expect mRNA or rRNA to...Ch. 9 - REFLECT AND APPLY Which would be more harmful to a...Ch. 9 - REFLECT AND APPLY Explain briefly what happens to...Ch. 9 - REFLECT AND APPLY Explain why a 50S ribosomal...Ch. 9 - Prob. 63RECh. 9 - Prob. 64RECh. 9 - Prob. 65RECh. 9 - Prob. 66RECh. 9 - RECALL What is the difference between miRNA and...Ch. 9 - Prob. 68RECh. 9 - Prob. 69RE
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- The titration curve of alanine shows the ionization of two functional groups with pK values of 2.34 and 9.69, corresponding to the ionization of the carboxyl and the protonated amino groups, respectively. The titration of di-, tri-, and larger oligopeptides of alanine also shows the ionization of only two functional groups, although the experimental pK values are different. The table summarizes the trend in pK values. Amino acid or peptide Ala Ala-Ala pKj pk₂ 2.34 9.69 3.12 8.30 Ala-Ala-Ala 3.39 8.03 Ala-(Ala)-Ala, n ≥ 4 3.42 7.94 Modify the molecules to show the oligopeptide Ala-Ala-Ala. You can modify the molecules by moving, adding, deleting, or changing atoms, bonds, or charges. C Select c Draw Templates More H с N 0 S Cl H H | | || H CH3 H CH, H CH₂ Complete the statements about the the pK, values of the Ala-Ala-Ala oligopeptide. The pK₁ value of 3.39 is associated with the -COO group of Ala-Ala-Ala. The pK2 value of 8.03 is associated with the -NH group of Ala-Ala-Ala. Erase Q2 Q…arrow_forwardFacts from the bacterium mals and to dept kan apa in a peptide with antidic properties. This peptide complex with the call membrance of other hacterial species, leading in bacterial death The structure of the peptide has been determined from (a) Cmplete acid hydes of the peptide, followed by amino acid analys, yielded quiar anunt of Lan, Om, Pfx, Prxa, and Wall Cmtiti, an amino acid od prosentin pockets but present in some peptides. Com has the tracture H *H,N-CH-CH-CH, -C- COO (b) The weight of the peptide in approximately 1,200 Th (c) The peptide failed to undergo hydrolysis when treated with the Hydrolysis of the carbonyl-terminal residue of a polypeptide une "NH, the year. This call there Pro or the police does not contain a froz (d) Treatment of the peptide with 1-haw-2,4-dicherer (11N1), followed by complete hydrolysis and ched only from and the derivative NO, Н ON NHCHI CH, CH, C coo +NH, (Hint: The 2,4-diphenyl derivative involves the amino group of a side chain rather than the…arrow_forwardElectrophoresis Macmillan Learning Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and lane 2 contains chymotrypsin pre-treated with performic acid. 1 2 Why does performic acid treatment of chymotrypsin generate three bands in lane 2? ° Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues. The three peptides are impurities in the original chymotrypsin sample. Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues. Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin. Correct Answerarrow_forward
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