4. Draw a chemical mechanism (with electron-pushing arrows) for how glycine isadded to a polypeptide as it is synthesized on the ribosome. Be sure to show theattacking nucleophile, the leaving group, and any intermediates in the chemicalreaction.

Ribosomes are protein-RNA complexes that catalyse peptide bond formation. A peptide bond is formed…

Answered: 4. Draw a chemical mechanism (with…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter15: From Dna To Protein

Section: Chapter Questions

Problem 4TYK

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1. What are two major similarities between protein synthesis in bacteria and eukaryotes? What aretwo major differences? 2. Is it reasonable to expect that protein degradation can take place at any location in a cell? 3. . In ubiquitination, chaperone can be part of the process. Explain the benefits of using chaperoneand differentiate the uses of chaperone and ubiquitin.
2. Phospholipases (PL) are enzymes that hydrolyzes PLA1 phospholipids into fatty acids and other lipophilic substances. Different class of phospholipase cleaves different bond in a phospholipid molecule. Shown on the right are the cleavage sites of four classes of PL: PLA1, PLA2, PLC, and PLD. R1 R2 -O-P-'·O-R3 (a) Write down the reaction of phosphatidylcholine (PC) cleaved by PLA2. Suppose the two acyl groups are R1 and R2 as shown in the figure. Make sure the chiral carbons in the reactions have the right stereochemistry (i.e., use wedge-dash notation), and the charges on the atoms reflect the molecule in neutral pH. PLA2 PLC PLD (b) Which PL is needed in order to release choline for salvage? (c) What is the structure and name of the remaining molecule after cleaving PC by the PL in (b) and releasing choline. No need to use wedge-dash notation. (d) The molecule in (c) can be used to synthesize triacylglycerol. Write down the reactions, including the enzymes and cofactors. Assume the…
1. Why does a cell use deoxyribonuclease?
10. A portion of 5'-AUGCCACGAGUUGAC-3'. What amino acid sequence does this code for? To answer the question please: I) explain what is the genetic code and list the properties of the genetic e 2) draw a diagram of protein synthesis; 3) determine which tRNA should be attached to the mRNA; 4) what is the anticodon for the very first tRNA that will attach to mRNA? mRNA molecule has the sequence an
1. The enzyme activity that forms peptide bonds on the ribosome is called peptidyl transferase. Explain which molecule catalyzes this reaction?
9. Put the following events in the synthesis of a polypeptide in the proper order. An initiator tRNA already bound to the small subunit binds to an mRNA. An aminoacyl tRNA matches its anticodon to the codon in the A site. The large subunit attaches to the small subunit, with the initiator tRNA in the P site. A peptide bond forms. A tRNA translocates from the A site to the P site, and an empty tRNA exits from the E site.
Which of the following statements is false? a. GTP is an energy source during various stages of translation. b. In the ribosome, peptidyl transferase catalyzes peptide bondformation between amino acids. c. When the mRNA code UAA reaches the ribosome, there isno tRNA to bind to it. d. A long polypeptide is cut off the tRNA in the A site so its Metamino acid links to the amino acid in the P site. e. Forty-two amino acids of a protein are encoded by 126nucleotides of the mRNA.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Energy that drives translation is provided mainly by ___ . a. ATP b. amino acids c. CTP d. all of the above
Figure 15.16 Many antibiotics inhibit bacterial protein synthesis. For example, tetracycline blocks the A site on the bacterial ribosome, and chloramphenicol blocks peptidyl transfer. What specific effect would you expect each of these antibiotics to have on protein synthesis? Tetracycline would directly affect: tRNA binding to the ribosome ribosome assembly growth of the protein chain Chloramphenicol would directly affect tRNA binding to the ribosome ribosome assembly growth of the protein chain
1. Considering the following nucleotide sequence in an mRNA molecule: 5’ AUG UUA CGU AAU GCU GUC GAA UCU AUU UGC UUU ACA UAA 3' d) Write the amino acid sequence of the peptide synthesized from the given mRNA nucleotide sequence. e) Draw the structure of the pertide fragment made up of the first five (5) amino acids in the given polypeptide.
5. E. coli ribonuclease H1 is an enzyme that catalyzes the hydrolysis of phosphodiester bonds in RNA. Its proposed mechanism involves a 'carboxylate relay,' as shown below. His124 Asp70 || -HN-CH-C -HN-CH-C- CH2 CH2 c=0 RNA substrate HN H. H. (1) Fill the blanks. In the reaction scheme above, His124 acts as a ( ). The purpose of this relay system is to deprotonate the water molecule (II) so that it becomes a better ( :0

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4. Draw a chemical mechanism (with electron-pushing arrows) for how glycine is added to a polypeptide as it is synthesized on the ribosome. Be sure to show the attacking nucleophile, the leaving group, and any intermediates in the chemical reaction.