Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 16, Problem 3VCQ
Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?
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A mutation that changes an alanine to a leucine in the nucleus of a protein leads to a less active one protein. However, the protein can be made active again by introducing another mutation into anotherpart of the protein where phenylalanine is replaced by alanine. How can it be thought of this othermutation leads to the activity being recovered?
The protein shown here is flavodoxin, which contains both alpha helices and beta sheets.
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protein tertiary structure
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Chapter 16 Solutions
Biology 2e
Ch. 16 - Figure 16.5 In E. coli, the tip operon is on by...Ch. 16 - Figure 16.7 In females, one of the two X...Ch. 16 - Figure 16.13 An increase in phosphorylation levels...Ch. 16 - Control of gene expression in eukaryotic cells...Ch. 16 - Post-translational control refers to: regulation...Ch. 16 - How does the regulation of gene expression support...Ch. 16 - If glucose is absent, but so is lactose, the lac...Ch. 16 - Prokaryotic cells lack a nucleus. Therefore, the...Ch. 16 - The a/a operon is an inducible operon that...Ch. 16 - What are epigenetic modifications? the addition of...
Ch. 16 - Which of the following are true of epigenetic...Ch. 16 - The binding of _____ is required for transcription...Ch. 16 - What will result from the binding of a...Ch. 16 - A scientist compares the promoter regions of two...Ch. 16 - Which of the following are involved in post...Ch. 16 - Binding of an RNA binding protein will the...Ch. 16 - An unprocessed pre-mRNA has the following...Ch. 16 - IS. Alternative splicing has been estimated to...Ch. 16 - Post-translational modifications of proteins can...Ch. 16 - A scientist mutates elF-2 to eliminate its GTP...Ch. 16 - Cancer causing genes are called transformation...Ch. 16 - Targeted therapies are used in patients with a set...Ch. 16 - Name two differences between prokaryotic and...Ch. 16 - Describe how controlling gene expression will...Ch. 16 - Describe how transcription in prokaryotic cells...Ch. 16 - What is the difference between a repressible and...Ch. 16 - In cancer cells, alteration to epigenetic...Ch. 16 - A scientific study demonstrated that rat mothering...Ch. 16 - Some autoimmune diseases show a positive...Ch. 16 - A mutation within the promoter region can alter...Ch. 16 - What could happen if a cell had too much of an...Ch. 16 - A scientist identifies a potential transcription...Ch. 16 - Describe how RBPs can prevent miRNAs from...Ch. 16 - How can external stimuli alter...Ch. 16 - Protein modification can alter gene expression in...Ch. 16 - Alternative forms of a protein can be beneficial...Ch. 16 - Changes in epigenetic modifications alter the...Ch. 16 - A scientist discovers a virus encoding a Protein X...Ch. 16 - New drugs are being developed that decrease DNA...Ch. 16 - How can understanding the gene expression pattern...
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- Phosphorylation is a common covalent modification of proteins in all forms of life, which leads to the question, What makes protein phosphorylation so valuable in regulating protein function that its use is ubiquitous?arrow_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_forwardHow many ATP and GTP molecules would be hydrolyzed in the synthesis of a 125 amino acid protein? Explain why this is a good argument for careful regulation of gene expression (especially considering that most proteins are larger than 125 amino acids).arrow_forward
- 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?arrow_forwardThe proteasome is a multi-subunit machine that unfolds and degrades proteins. How is its activity regulated such that it only degrades certain proteins?arrow_forwardProkaryotes and eukaryotes have different Ribosomes that are involved in this process. Which type of cells express the 50S subunit? How have we used this in medicine?arrow_forward
- A cell has a defective enzyme that attaches the alanine amino acid (Ala), instead of a valine amino acid (Val), to tRNAs with the anticodon CAA. Will any polypeptides in the cell contain valine? Why or why not?arrow_forwardA mutation that changes an alanine residue in a protein to an isoelectric, lead to a loss of activity. Activity is regained when a further mutation at the same site changes isoleucine to a glycine. Why?arrow_forwardAfter the GEF causes the GTPase to release its GDP, why is the nucleotide-binding site immediately filled by a GTP molecule rather than a GDP molecule?arrow_forward
- A mutation that changes an alanine residue in the interior of a protein to valine is found to lead to a loss of activity. However, activity is regained when a second mutation at a different position changes an isoleucine residue to glycine. How might this second mutation lead to a restoration of activity?arrow_forwardThe first successful drug trial to reduce concentrations of huntingtin in the brain used single stranded DNA molecules. Suggest and explain how this drug could cause a reduction in the concentration of the protein huntingtin.arrow_forwardFigure 1 represents the amino acid sequence of a G-protein coupled receptor (GPCR) as determine by mass spectrometry. *Figure 1 is shown as in the added image. Figure 1: The amino acid sequence of a GPCR as determined by mass spectrometry. a) Describe a spectroscopic technique that you can use to determine the structure of the GPCR apart from mass spectrometry.arrow_forward
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