WORLD OF CELL+ACCESS CODE >CUSTOM<
17th Edition
ISBN: 9781323628669
Author: Hardin
Publisher: PEARSON C
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Chapter 19, Problem 19.4CC
Enzymes can undergo allosteric regulation or regulation by covalent modification (see Chapter 6). Which category do posttranslational modifications fall into?
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Explain the term posttranslational modifications?
One single polypeptide chain (120 amino acid residues) is produced for protein A in prokaryotic cell. N-terminal amino acid is alanine in the chain of this protein. How many moles of ATP and GTP will be in use for this polypeptide chain synthesis? What post-translational modifications may be for this protein?
Chapter 19 Solutions
WORLD OF CELL+ACCESS CODE >CUSTOM<
Ch. 19 - Suppose a tRNA has the anticodon 3-CGU-5. What two...Ch. 19 - Kanamycin is an antibiotic that binds to bacterial...Ch. 19 - You are working in a lab to identify new alleles...Ch. 19 - Suppose you are using GFP fusion proteins to study...Ch. 19 - Enzymes can undergo allosteric regulation or...Ch. 19 - Suppose you use molecular biology techniques to...Ch. 19 - Prob. 19.1PSCh. 19 - Tracking a Series of Mutations. The following...Ch. 19 - Prob. 19.3PSCh. 19 - Prob. 19.4PS
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Distinguish allosteric regulation and covalent modificationarrow_forwardPlease answer both questions: a) If we get 36 ATPs in the complete oxidation of one molecule of glucose, how many amino acid residues can be incorporated to a growing polypeptide chain using the energy derived from glucose. Show how you arrived at your answer. b) All polypeptide synthesis starts with the codon AUG bringing methionine at the very first position at the N terminal but, examination of many biological and functional proteins in the cell, when sequenced, does not reveal the presence of methionine at the very first position at the N-terminal. Why and how could this be possible? Explain.arrow_forwardMany blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?arrow_forward
- Post-translational modification of proteins refers to the covalent and enzymatic modification of proteins following protein biosynthesis. Give three (3) examples and briefly describe why the modification is important.arrow_forwardWhich of the following could create different versions of an enzyme? (Select all that apply) Note: by "versions" we mean isoforms with similarity but also some differences in their polypeptide sequence Group of answer choices reciprocal regulation allosteric activation substrate concentration a gene is duplicated and the 2 copies evolve different changes over time alternative splicingarrow_forwardBriefly (list in bullet points) what are the FIVE stages of Protein synthesis. Why do you suppose incidences of mutations in enzymes involved in these processes are extremely rare in people — affectingarrow_forward
- Define the following terms: a. posttranslational modification b. transpeptidation c. translocation d. termination e. targetingarrow_forwardWhat kinds of effects can occur on cellular metabolism when we introduce genetic modifications into a cell? And why does yeast produce ethanol?arrow_forwardCompare and contrast the metabolic pathways leading to thymine in DNA and thymine as a modified base in tRNA.arrow_forward
- Human ribonucleotide reductase has two allosteric sites, the S site and the A site. What is the function of each? How does this compare with the E. Coli enzyme discussed in the text?arrow_forwardExplain the critically important role of aminoacyl-tRNA synthetases in protein synthesis.arrow_forwardThe synthesis of a protein requires that the amino acids that constitute the growing polypeptide chain be covalently linked to the amino acid attached to the tRNA at the aminoacyl site of the ribosome. Which of the following catalyses this reaction? Options: the aminoacyl tRNA synthetase eEF2 eEF1-GTP a large ribosomal RNA the initiator tRNA metarrow_forward
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