Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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As we focused on the translation of mRNA into proteins as well as on protein structure and function. Along the way, we found many opportunities to consider the methods and reasoning by which much of this information
was acquired. From the explanations given in the chapter,
what answers would you propose to the following fundamental
question
What experimentally derived information led to Holley’s
proposal of the two-dimensional cloverleaf model of tRNA?
Expert Solution
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Step 1
tRNA : It is an adaptor molecule composed of RNA, typically nucleotides in length, that serves as the physical link between the mRNA and the amino acid sequence of proteins.
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- Explain the interactions of specific tRNA with its synthetase, by including the importance of cloverleaf structure of tRNA, which domains are involved, distinct recognition sites, D-arm, TψC arm, anticodon loop and stem, linkage, activation, amino acceptor arm, ensuring the correct tRNA to be recognized by its synthetase. Please do not answer with an incredibly long reply. I would just like the most condensed answer possible by providing all key points asked about. Thanks!arrow_forwardWhat steps are required to form a charged tRNA?arrow_forwardWhat amino acid would a tRNA with anticodon CUA carry? Enter the 3 letter code only [A]. [e.g. Met for anticodon UAC]arrow_forward
- What is an anticodon and where is it located on the tRNA structure?arrow_forwardIn the absence of cladosporin, explain the elongation steps in the synthesis of lysyl-tRNA synthetase enzyme or protein in bacterial cells by including any elongation factors, base pairing of codon/anticodon, any conformational shift, proofreading, any hydrolysis, exchange, ribosomal subunits involved, charged tRNA, peptide bond formed. This question does not require a super long in depth answer, a short to the point answer is preferred if possible. Thank you!arrow_forwardName the four classes of RNA and briefly explain their functional significance. In what reaction(s) do they participate?arrow_forward
- In regard to the wobble hypothesis and the fact that cells do not need a full complement of tRNAs for codons. What would the consequences be if a cell lost the tRNA gene with the following anticodon sequences Please explain in depth A. 3'-ACA-5' B. 3'-CUG-5'arrow_forwardWhat are two possible anticodon sequences for tRNA's that are charged with Phenylalanine (Phe)? O 3' AAU 5' and 3' GAA 5' O 3' AAA 5' and 3' AAG 5 3' UUG 5' and 3' CUG 5' O 3' GAA 5' and 3' CAG 5' 3' GUA 5' and 3' GUG 5'arrow_forwardExamine the tRNA in Figure 15.14. What do you think would be the potential effect of a mutation in the part of the tRNA gene that encodes (a) the acceptor stem; (b) the anticodon; (c) one of the red nucleotide positions?arrow_forward
- IX. Dibuje la estructura del polinucleótido que aparece a continuación el cual corresponde a un codón en el mRNA que codifica para el aminoácido prolina. (Solamente se pide el dibujo de la estructura siguiendo el modelo de polinucleótido mostrado en clase). e). .) 5'-C-C-C-3' Show Transcribed Text IX. Draw the structure of the polynucleotide below which corresponds to a codon in the mRNA that codes for the amino acid proline. (Only a drawing of the structure following the polynucleotide model is requested)arrow_forwardExplain how lysyl-tRNA synthetase protein in bacterial cells typically undergoes folding with necessary structures and steps, any ATP hydrolysis, cap structure, etc.arrow_forwardTreating 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 activityarrow_forward
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