Essentials of Genetics (9th Edition) - Standalone book
9th Edition
ISBN: 9780134047799
Author: William S. Klug, Michael R. Cummings, Charlotte A. Spencer, Michael A. Palladino
Publisher: PEARSON
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Chapter 12, Problem 5PDQ
In studies using repeating
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TRUE OR FALSE
a) The structure of the purines and pyrimidines make them able to undergo keto-enol tautomerism.
b) A unique 5'CCA terminal sequence is found in all tRNAs to be able to carry the correct amino acid to the ribosome.
Which of the following statements regarding Anfinsen's denaturing experiments with ribonuclease A are valid?
(i) Exposing the denatured protein to air oxidation and then dialysis to remove urea restored the protein to its original functionality.
(ii) Removing urea by dialysis and then allowing air oxidation of the denatured protein restored the protein to its original functionality.
(iii) Denaturing the protein with both urea and β-mercaptoethanol yielded an inactive protein.
(iv) Protein folding is determined by its primary sequence.
The antibiotic cordycepin inhibits bacterial RNA synthesis. Solve, (a) Of which nucleoside is cordycepin a derivative? (b) Explain cordycepin’s mechanism of action.
Chapter 12 Solutions
Essentials of Genetics (9th Edition) - Standalone book
Ch. 12 - CASE STUDY | A drug that sometimes works A...Ch. 12 -
CASE STUDY | A drug that sometimes works
A...Ch. 12 -
CASE STUDY | A drug that sometimes works
A...Ch. 12 - HOW DO WE KNOW? In this chapter, we focused on the...Ch. 12 - Review the Chapter Concepts list on p. 215. These...Ch. 12 - In studies of frameshift mutations, Crick,...Ch. 12 -
4. The mRNA formed from the repeating...Ch. 12 - In studies using repeating copolymers, AC......Ch. 12 - Prob. 6PDQCh. 12 - Prob. 7PDQ
Ch. 12 -
8. When the amino acid sequences of insulin...Ch. 12 - Prob. 9PDQCh. 12 - Why doesn't polynucleotide phosphorylase (Ochoa's...Ch. 12 - Refer to Table 12.1. Can you hypothesize why a...Ch. 12 -
12. Predict the amino acid sequence produced...Ch. 12 - A short RNA molecule was isolated that...Ch. 12 - A glycine residue exists at position 210 of the...Ch. 12 - Shown here is a theoretical viral mRNA sequence...Ch. 12 -
16. Most proteins have more leucine than...Ch. 12 - Define the process of transcription. Where does...Ch. 12 - Describe the structure of RNA polymerase in...Ch. 12 - In a written paragraph, describe the abbreviated...Ch. 12 - Messenger RNA molecules are very difficult to...Ch. 12 - One form of posttranscriptional modification of...Ch. 12 - In a mixed copolymer experiment, messages were...Ch. 12 -
23. Shown in this problem are the amino acid...Ch. 12 - Alternative splicing is a common mechanism for...Ch. 12 - The genetic code is degenerate. Amino acids are...
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- A heptapeptide was found to have an amino acid composition of Asp, Leu, Lys, 2 Met, Phe and Tyr. (a) Trypsin has no effect on the heptapeptide. (b) The phenyl thiohydantoin released by Edman degradation revealed phenylalanine in the N-terminus. (c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. (d) Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys. What is the amino acid sequence of this heptapeptide? Answer Format: (Three letter abbreviation with dash ie., Ala-Gly-…) *arrow_forwardThe majority of bacterial mutations that need isoleucine also require valine for growth. Why? Which enzyme or process would be deficient in a mutant that requires solely isoleucine for growth (rather than valine)?arrow_forwardThe objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…arrow_forward
- Explain the nucleoside diphosphates (NDPs) ? How it is formed ?arrow_forwardHow does the aminoacyl-tRNA synthetase that attaches the amino acid proline know which tRNA to attach the proline to?Question 24 options: A) the synthetase recognizes the sequence of the first 3 bases on the 3' end of the tRNA B) the synthetase reads the anticodon as well as a few other unique bases in tRNAPro C) proline only fits into the 3-dimensional structure of the tRNAPro D) the synthetase randomly chooses a tRNAarrow_forwardMost bacterial mutants that require isoleucine for growth also require valine.Why? Which enzyme or reaction would be defective in a mutant requiringonly isoleucine (not valine) for growth?arrow_forward
- Draw the structure of a phosphonamidite monomer suitable for SPPS of adenosine RNA Nucleosides. Circle all protecting groups and identify their canonical deprotection conditions.arrow_forwardConsider the peptide Asp-Lys-Phe-Glu-Asn-Tyr-Gln-Val-Cys. In a single beaker, you treat this peptide with 2 proteases. One protease cleaves at the N-terminus of aromatic R groups and the other cleaves at the C-terminus of polar, non-ionizable R groups. Following the enzymatic digestion, you want to separate your peptide fragments so that you can identify them. You choose to separate the fragments using an anion exchange column. Beginning at pH=6 you apply your peptide fragments to the column and you gradually decrease the pH of the column stopping the separation when the pH of the column equals 4. Omitting chemical structures, write the amino acid sequence of the peptide fragments that are produced from this digest. Write the order that these fragments will elute from the column (if at all). (Relevant pKa values are: 2.1, 3.8, 4.3, 8.3, 9.6, 10.1, and 10.5)arrow_forwardThe following polynucleotide was synthesized and used as a template forpeptide synthesis in a cell-free system from E. coli. …AUAUAUAUAUAUAU…What polypeptide would you expect to be produced? What informationwould this give you about the code?arrow_forward
- Wild-type E. coli cells can synthesize all 20 common amino acids, but some mutants, called amino acid auxotrophs, are unable to synthesize a specific amino acid and require its addition to the culture medium for optimal growth. Besides their role in protein synthesis, some amino acids are also precursors for other nitrogenous cell products. Consider the three amino acid auxotrophs that are unable to synthesize glycine, glutamine, and aspartate, respectively. Match each nitrogenous product with the mutant or mutants that would fail to synthesize it. Each mutant may fail to synthesize more than one nitrogenous product, and some nitrogenous products may fail to be synthesized by more than one mutant. glycine auxotrophs glutamine auxotrophs aspartate auxotrophs Answer Bank adenine nucleotides cytosine nucleotides guanine nucleotides uridine nucleotidesarrow_forward1. A) Explain this statement, “Most enzymes are gene-encoded proteins, but most enzymes are not only protein". B) You recently isolated a new enzyme in your lab, and you named it "lipidase 1120". As a temporary name, this is fine. Who is responsible for assigning a formal name, and on what criteria will that name be assigned?arrow_forwardThe genetic code was deciphered by experiments in which synthetic polyribonucleotides of known repeating sequences were used as mRNAs to direct protein synthesis in cell - free extracts . What type or types of polypeptides would you expect to be synthesized if poly (AAG) n (A) AAGAAGAAG ) used as the template for in vitro peptide synthesis ?arrow_forward
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