Human Anatomy & Physiology (2nd Edition)
2nd Edition
ISBN: 9780134553511
Author: Erin C. Amerman
Publisher: PEARSON
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Chapter 3.7, Problem 5QC
Why is posttranslational modification necessary for a protein to be functional?
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Chapter 3 Solutions
Human Anatomy & Physiology (2nd Edition)
Ch. 3.1 - What general processes are carried out by cells?Ch. 3.1 - Prob. 2QCCh. 3.1 - Where are intracellular and extracellular fluids...Ch. 3.2 - 1. How do phospholipids arrange themselves in the...Ch. 3.2 - 2. How is the plasma membrane described according...Ch. 3.2 - 3. What are five functions of membrane proteins?
Ch. 3.2 - What roles do cholesterol, glycoproteins, and...Ch. 3.3 - Mark each of the following statements as true or...Ch. 3.3 - Mark each of the following statements as true or...Ch. 3.3 - Mark each of the following statements as true or...
Ch. 3.3 - Mark each of the following statements as true or...Ch. 3.3 - How does the process of primary active transport...Ch. 3.3 - What is the main primary active transport pump in...Ch. 3.3 - 7. How does the process of secondary active...Ch. 3.3 - Prob. 8QCCh. 3.3 - Explain the basic process of exocytosis.Ch. 3.4 - 1. Identify the properties listed in the next...Ch. 3.4 - Identify the following properties as belonging to...Ch. 3.4 - To what destinations can products from the Golgi...Ch. 3.5 - Prob. 1QCCh. 3.5 - Prob. 2QCCh. 3.5 - Prob. 3QCCh. 3.6 - 1. What are the main components of the nucleus?...Ch. 3.6 - What is chromatin? How are chromatin and...Ch. 3.6 - 3. What is a nucleolus, and what is its...Ch. 3.7 - How is a codon related to a triplet?Ch. 3.7 - 2. Describe the basic steps of transcription.
Ch. 3.7 - Explain how tRNA acts as the translator of the...Ch. 3.7 - Describe the basic steps of translation.Ch. 3.7 - 5. Why is posttranslational modification...Ch. 3.7 - 6. Why is it important to regulate gene...Ch. 3.8 - What happens during each stage of the cell cycle?Ch. 3.8 - What does semiconservative replication mean?Ch. 3.8 - Describe the changes in the cell that take place...Ch. 3.8 - What are four external factors that play a role in...Ch. 3 - Which of the following is not a basic function...Ch. 3 - Prob. 2CYRCh. 3 - What are the two fluid compartments in the body,...Ch. 3 - 4. Which of the following best describes the...Ch. 3 - Mark the following statements about the plasma...Ch. 3 - 6. What is the primary difference between active...Ch. 3 - 7. Match the term with its appropriate...Ch. 3 - 8. Fill in the blanks: A hypotonic solution will...Ch. 3 - 9. Match the following terms with the correct...Ch. 3 - Prob. 10CYRCh. 3 - Mark the following statements about the...Ch. 3 - 12. Our somatic cells’ DNA is distributed among...Ch. 3 - Explain how and why chromatin is condensed in the...Ch. 3 - Which of the following statements correctly...Ch. 3 - Each of the following statements about protein...Ch. 3 - Number the following steps of protein synthesis in...Ch. 3 - Which of the following is not a phase of mitosis?...Ch. 3 - 18. Why is regulation of the cell cycle...Ch. 3 - 19. Mark the following statements about the cell...Ch. 3 - 20. Match the following terms with the correct...Ch. 3 - 1. Write a single sentence, using no more than 25...Ch. 3 - 2. Certain diseases are transmitted via...Ch. 3 - 3. Explain how the form of each of the following...Ch. 3 - Certain types of cancerous lung tumors can secrete...Ch. 3 - Why do you think the rate of cell division is...Ch. 3 - 1. A patient is admitted to the hospital and...Ch. 3 - A popular science fiction program once had an...Ch. 3 - Prob. 3AYKACh. 3 - Prob. 4AYKACh. 3 - The drug methotrexate is used to treat several...
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- What advantages are there for synthesizing an inactive protein that must subsequently be activated by posttranslationalmodifications?arrow_forwardwhat is post-translational protein covalent modification? give three examples and name the enzyme that catalyzes each reaction.arrow_forwardBriefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)arrow_forward
- Many 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_forwardWhy is post translational modification important and Where does protein modification occur?arrow_forwardWhat is post-translational modification? Describe two specific post-translational modifications and one effect of each modification?arrow_forward
- Posttranslational modifications serve several purposes. Discuss and give examplesarrow_forwardWhen glycoproteins are synthesized in the cell, at what stage of the polymerization of the protein are the sugar groups added: Prior to translation, cotranslationally, or posttranslationally?arrow_forwardWhen the amino acid sequences of insulin isolated from different organisms were determined, differences were noted. For example, alanine was substituted for threonine, serine for glycine, and valine for isoleucine at corresponding positions in the protein. List the single-base changes that could occur in codons of the genetic code to produce these amino acid changes.arrow_forward
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