Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 9, Problem 11RQ
What property enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated?
- They are polar.
- They are non-polar.
- They contain a hydroxyl group.
- They occur more frequently in the amino acid sequence of signaling proteins.
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d) Alcohols usually don't behave as a weak acids, but tyrosine does. Explain why Y
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f)
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Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two
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Chapter 9 Solutions
Biology 2e
Ch. 9 - Figure 9.8 HER2 is a receptor tyrosine kinase. In...Ch. 9 - Figure 9.10 In certain cancers, the GTPase...Ch. 9 - Figure 9.17 Which of the following statements...Ch. 9 - Figure 9.18 What advantage might biofilm...Ch. 9 - What property prevents the ligands of cell-surface...Ch. 9 - The secretion of hormones by the pituitary gland...Ch. 9 - Why are ion channels necessary to transport ions...Ch. 9 - Endocrine signals are transmitted more slowly than...Ch. 9 - A scientist notices that when she adds a small,...Ch. 9 - Where do DAG and IP3 originate? They are formed by...
Ch. 9 - What property enables the residues of the amino...Ch. 9 - Histamine binds to the H1 G-protein-linked...Ch. 9 - A scientist observes a mutation in the...Ch. 9 - What is the function of a phosphatase? A...Ch. 9 - How does NF-kB induce gene expression? A small,...Ch. 9 - Apoptosis can occur in a cell when the cell is...Ch. 9 - What is the effect of an inhibitor binding an...Ch. 9 - How does PKC’s signaling role change in response...Ch. 9 - A scientist notices that a cancer cell line fails...Ch. 9 - Which type of molecule acts as a signaling...Ch. 9 - Quorum sensing is triggered to begin when...Ch. 9 - A doctor is researching new ways to treat biofilms...Ch. 9 - What is the difference between intracellular...Ch. 9 - How are the effects of paracrine signaling limited...Ch. 9 - What are the differences between internal...Ch. 9 - Cells grown in the laboratory are mixed with a dye...Ch. 9 - Insulin is a hormone that regulates blood sugar by...Ch. 9 - The same second messengers are used in many...Ch. 9 - What would happen if the intracellular domain of a...Ch. 9 - If a cell developed a mutation in its MAP2K1 gene...Ch. 9 - What is a possible result of a mutation in a...Ch. 9 - How does the extracellular matrix control the...Ch. 9 - A scientist notices that a cancer cell line shows...Ch. 9 - What characteristics make yeasts a good model for...Ch. 9 - Why is signaling in multicellular organisms more...Ch. 9 - Pseudomonas infections are very common in hospital...
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- Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. The saccharide was cleaved from its sialic acid residues. The treatments and results are as follows: 1. hydrolysis by B(1-> 4) - disaccharide products 2. hydrolysis by a(1-> 4) - release of 2 disaccharide & 2 monosaccharide units. Show the structure of the saccharide.arrow_forwardDiisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195. Which statement is true of DIPF's inhibitory mechanism? DIPF randomly modifies all serine residues on the protein, and if enough is added, the serine in the active site will eventually be modified. DIPF approaches serine 195 more closely than other substrates. DIPF looks like the substrate for chymotrypsin and binds in the active site as a competitive inhibitor. Serine 195 is in an environment that gives it a higher than normal reactivity with respect to DIPF.arrow_forwardH CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14arrow_forward
- Consider, for example, that a particular serine residue is phosphorylated to activate the protein. In the lab, a similar effect is achieved by mutating this residue to either a D (aspartic acid) or E (glutamic acid). What could be the reason?arrow_forwardSynthesis of peptide bonds is [exorgonic or endergonic]. Thus in isolation, this reaction would [occur or not occur] in cells. Peptide synthesis at the ribosome is coupled to GTP hydrolysis which is an [exergonic or endergonic] process thus making the overall process of synthesizing peptides [spontaneous or not spontaneous].arrow_forwardSnake venom contains many hydrolase enzymes, including several serine proteases. One such protease (present in high concentrations in snake venom) mimics the action of thrombin to activate fibrin. The venom protease cleaves peptide bonds with a specificity for basic, positively charged amino acids. This enzyme is incubated with a substrate peptide with the sequence SNPDCKVALYMTW. Draw a mechanism for the peptide hydrolysis of this specific peptide catalyzed by this snake venom protease. Include the structure of the active site amino acids of the enzyme and the substrate peptide group (including the full structure of the 2 specific amino acids that contribute to the scissile peptide group in the substrate) in your mechanism. Use the curved arrow convention to illustrate the flow of electrons.arrow_forward
- What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?arrow_forwardYou have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme's inactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by the absence of the S1 binding pocket. replacement of serine 195 with a positively charged residue. presence of a positively charged residue in the S1 binding pocket. presence of a negatively charged residue in the S1 binding pocket.arrow_forwardTPCK is a molecule with large hydrophobic groups. Why does TPCK inactivate chymotrypsin but not trypsin? TPCK looks like the substrate for chymotrypsin, but not trypsin, and thus can bind in its active site and modify His-57. Trypsin does not have a His residue present in the active site to react with TPCK. TPCK is a transition state analog for chymotrypsin, but not trypsin. TPCK binds to trypsin but does not modify its active site.arrow_forward
- Trypsin cleaves proteins on the carboxyl side of lysine. Trypsin inhibitor has a lysine residue, and binds to trypsin, yet it is not a substrate. Explain.arrow_forwardReceptor tyrosine kinases such as the epidermal growth factor (EGF) receptor can basically be broken down into three domains: (1) An extracellular, ligand binding domain, (2) A transmembrane domain that must cross through the cell membrane, and (3) an intracellular domain. Match the amino acid with the domain that it would MOST LIKELY be associated with. Lysine (choose (1), (2), or (3) from above) A tyrosine residue capable of being phosphorylated on its hydroxyl group (choose (1), (2), or (3) from above) Isoleucine (choose (1), (2), or (3) from above)arrow_forwardBased on the structure of CBB G-250, explain why it can bind to proteins having basic and hydrophobic amino acid residues.arrow_forward
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