38. Adenosine deaminase acting on RNA(ADARS) catalyzes the conversion ofAdenosine to Inosine (at right). This is anRNA editing enzyme. Why does A to Iediting destabilize duplex RNA? Draw outhow inosine could base pair with cytosine(Draw hydrogen bonds as dashed lines,and draw hydrogen atoms involved inhydrogen bonds. Indicate the position of the ribose with an "R" (you do not need to drawthe ribose).ADARNH2 EditingN-enzymeN-NHN.N.N.RNARNAAdenosineInosine

During the purine metabolism, the amino group from adenosine is removed by the enzyme adenosine…

Answered: 38. Adenosine deaminase acting on RNA…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Why RNase H cannot remove all the RNA residue from Okazaki fragments to form a lagging strand? Explain.
36.Start with two exons and an intervening intron. Include the cap and poly-A tail in your starting pre-mRNA. Show 2’-OH, 3’-OH, O-P-O phosphodiester bonds for the two transesterification reactions that splice exon 1 and exon 2. Be sure to include the branchpoint A and intron consensus sequences. You will need to show where the incoming -OH attacks the O-P-O bond to allow correct splicing in the lariat and between exons. Make your arrows precise. Show the lariat with the consensus sequences. Whenever possible, show 5’ and 3’ ends. Explain the fate of the lariat after it forms?
37. A portion of an mRNA attached to a ribosome reads: 5′ UUUGACCCCACG 3′ If a tRNA with an aspartic acid amino acid attached is in the P site of the ribosome, a tRNA with which amino acid attached will enter the A site? What amino acid will be attached to the amino group of the histidine encoded by this mRNA?
Identify each tertiary structure shown below. Draw the chemical mechanism for base-catalyzed RNA hydrolysis.
51. Prokaryotic RNAP requires four types of ribonucleoside triphosphates, a DNA molecule and a divalent metal atom. Please explain how each of these requirements support the function of RNAP.
Match the following (Most appropriate combinations only): IF1 IF3 IRES Shine-Dalgarno sequence m7-G Cap aminoacyl tRNA synthetase proofreading elF4E [Choose ] Binds ribosome A site Translation initiation in eukaryotes Translation initiation in Bacteria binds mRNA cap in eukaryotes Binds ribosome E site Correct charging of a tRNA with amino acid Cap-independent translation initiation of some viral mRNAs [Choose ] [Choose ] [Choose ] [Choose ]
Here is a DNA template strand’s sequence and direction: 3’-TACGCGGTAATC-5’ . What is the sequence and direction of mRNA synthesized from this DNA?
51 23. Suppose that a mutation occurs in the DNA sequence (indicated by a red nucleotide). 5 ATG GGA CCC CAT TCC GCC AAG GGG CAC TGA 3' 3 TAC CCT GGG GTA AGG CGG TTC CCC GTG ACT 5' Type the RNA sequence that would be produced by this template: 3′
Trypsin cleaves a polypeptide backbone at the C-terminal side of Arg or Lys residues, whereas chymotrypsin cleaves after aromatic residues. A polypeptide was treated with trypsin to generate a series of fragments of the following sequences: Gly-Gly-Ile-Arg Ser-Phe-Leu-Gly Trp-Ala-Ala-Pro-Lys Ala-Glu-Glu-Gly-Leu-Arg And the same polypeptide was treated with chymotrypsin to generate the following fragments: Leu-Gly Ala-Glu-Glu-Gly-Leu-Arg-Trp Ala-Ala-Pro-Lys-Gly-Gly-Ile-Arg-Ser-Phe Assemble the protein sequence.
Treating a solution of ribonuclease with 2-mercaptoethanol and urea denatures the enzyme. If the 2-mercaptoethanol is removed, followed by the removal of urea, the ability of the enzyme solution to hydrolyse RNA is reduced by about 99%. What is the most plausible explanation for this observation? a. All of the RNase molecules have about 1% of their usual activity, due to changes to the organisation of disulphide bonds b. Random formation of disulphide bonds mean about 1% of the RNase molecules are 100% active whereas 99% have no activity c. Deprotonation of histidine in the active site of the enzyme means that only about 1% of the enzyme molecules are active d. Deprotonation of histidine in the active site of the enzyme means that all of the enzyme molecules have 1% of their usual activity
Posttranslational modifications of proteins do not include: peptide bond formation glycosylation acetylation of N-terminal peptide bond cleavage disulfide bond formation QUESTION 16 14 15 16 streptomycin puromycin 17 18 19 20 Which one of the following antibiotics does NOT function by interfering with the translational/post-translation process tunicamycin penicillin O tetracyclin O O
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