Pearson eText Human Physiology: An Integrated Approach -- Instant Access (Pearson+)
8th Edition
ISBN: 9780135212905
Author: Dee Silverthorn
Publisher: PEARSON+
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Textbook Question
Chapter 2, Problem 26RQ
The graph shown below represents the binding of oxygen molecules (O2) to two different proteins, myoglobin and hemoglobin, over a range of oxygen concentrations. Based on the graph, which protein has the higher affinity for oxygen? Explain your reasoning.
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One molecule of 2,3-bisphosphoglycerate (BPG) binds to one molecule of haemoglobin (Hb) in a central cavity of the haemoglobin molecule. Is the interaction between BPG and Hb stronger or weaker than it would be if BPG were bound to the surface of the protein instead? Explain your answer.
The Hb Yakima variation is caused by the mutation D99H, which results in a
shift in oxygen binding as shown in the graph. What effect does the D99H
variation have on the [T] / [R] ratio of Hb Yakima protein conformation
compared to Hb Normal and how does D99H alter oxygen affinity?
Fractional saturation
1.0
2
Hb Yakima
20
Hb Normal
40
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po, (kPa)
80
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solve the question given in the image provided.
Chapter 2 Solutions
Pearson eText Human Physiology: An Integrated Approach -- Instant Access (Pearson+)
Ch. 2.1 - List three major essential elements found in the...Ch. 2.1 - What is the general formula of a carbohydrate?Ch. 2.1 - Prob. 3CCCh. 2.1 - Prob. 4CCCh. 2.1 - Prob. 5CCCh. 2.1 - Prob. 6CCCh. 2.2 - Which dissolve more easily in water, polar...Ch. 2.2 - Prob. 8CCCh. 2.2 - Why does table salt (NaCl) dissolve in water?Ch. 2.2 - Prob. 10CC
Ch. 2.2 - pH is an expression of the concentration of what...Ch. 2.2 - Prob. 12CCCh. 2.3 - Prob. 13CCCh. 2.3 - Prob. 14CCCh. 2.3 - Match each chemical to its action(s).Ch. 2.3 - What happens to the rate of an enzymatic reaction...Ch. 2.3 - What happens to the rate of an enzymatic reaction...Ch. 2 - Prob. 1CRQCh. 2 - Prob. 2CRQCh. 2 - Prob. 3CRQCh. 2 - Prob. 4CRQCh. 2 - Name the element associated with each of these...Ch. 2 - Write the one- or two-letter symbol for each of...Ch. 2 - Prob. 7CRQCh. 2 - Prob. 8CRQCh. 2 - H+ is also called a proton. Why is it given that...Ch. 2 - Prob. 10CRQCh. 2 - Prob. 11CRQCh. 2 - Prob. 12CRQCh. 2 - Prob. 13CRQCh. 2 - Prob. 14CRQCh. 2 - Prob. 15CRQCh. 2 - What aspect of protein structure allows proteins...Ch. 2 - Prob. 17CRQCh. 2 - List the three components of a nucleotide.Ch. 2 - Compare the structure of DNA with that of RNA.Ch. 2 - Distinguish between purines and pyrimidines.Ch. 2 - Prob. 1RQCh. 2 - Prob. 2RQCh. 2 - Prob. 3RQCh. 2 - Prob. 4RQCh. 2 - Fill in the blanks with the correct bond type. In...Ch. 2 - Prob. 6RQCh. 2 - Prob. 7RQCh. 2 - Prob. 8RQCh. 2 - Prob. 9RQCh. 2 - Prob. 10RQCh. 2 - Prob. 11RQCh. 2 - A molecule that binds to another molecule is...Ch. 2 - Prob. 13RQCh. 2 - Prob. 14RQCh. 2 - Prob. 15RQCh. 2 - Prob. 16RQCh. 2 - A solution in which [H+] = 103 M is...Ch. 2 - Prob. 18RQCh. 2 - Prob. 19RQCh. 2 - Prob. 20RQCh. 2 - Prob. 21RQCh. 2 - Prob. 22RQCh. 2 - Prob. 23RQCh. 2 - Prob. 24RQCh. 2 - Prob. 25RQCh. 2 - The graph shown below represents the binding of...
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- Hemoglobin (Hb) is a blood protein that is responsible for transporting oxygen. It can exist in the protonated form as HbH*. The binding of oxygen can be represented by the simplified equation HbH+ + 02 > ABO2 + Ht A. Excessive vomiting may lead to metabolic alkalosis, in which [H2O*] in blood decreases. How does this condition affect the ability of Hb to transport O2? B.Diabetes mellitus may lead to metabolic acidosis, in which [HgO*] in blood How does this condition affect the ability of Hb to transport O?arrow_forwardYou have discovered a new form of mouse myoglobin that has a p50 of 9 Torr. At approximately what pO2 would this hemoglobin be 86% saturated with oxygen? 85 Torr 40 Torr 60 Torr 55 Torr Not enough information is given to answer this questionarrow_forwardAmino acid substitutions at the interfaces of the a and B subunits of hemoglobin can change the relative stability of the oxy (R) and deoxy (T) forms of the molecule. In one mutant hemoglobin molecule a hydrogen bond involved in stabilizing the R form of the molecule is lost. As a result, would expect this mutant hemoglobin to have a higher or lower affinity for oxygen as a ligand. Explain.arrow_forward
- Identify the incorrect statement regarding the polypeptide, Myoglobin. Select one: a. The interaction between Myoglobin and O2 is homotopic in nature as indicated by a Hill coefficient n = : 1 b. Myoglobin is found predominantly in muscle tissue because it facilitates oxygen diffusion. c. The majority of Myoglobin's secondary structure is composed of alpha-helices d. Myoglobin has a higher affinity for oxygen than Hemoglobin e. Myoglobin serves as an oxygen storage protein as suggested by its hyperbolic binding of 02arrow_forwardA red heme-containing protein called leghemoglobin is found in the nitrogen-fixing root nodules of leguminous plants. The protein component is produced by the plant, whereas bacterial cells produce the precursor of heme. Can you deduce the function of leghemoglobin? [Hint: Leghemoglobin is a member of the globin superfamily.]arrow_forwardWhich of the following is not an example of a protein with a quaternary structure? Haemoglobin in adult humans has the composition aa2ßß2. Myoglobin, an oxygen-binding protein in muscle, consists of a single subunit. Calmodulin is a Ca2+ -binding protein which is formed by two identical subunits. The photosynthetic enzyme Rubisco is composed of 8 L subunits and 8 S subunits.arrow_forward
- The Graph below shows the binding curves of two proteins (A and B) for the same ligand (L). Use this Graph and determine the dissociation constant, K, for both proteins. Which protein (A or B) has a greater affinity for ligand L? Which of the two proteins would be more easily inhibited by an antagonist? 1.0 Y 0.5 2 A 4 6 B 8 [L] (μM) 10 12 14 16arrow_forwardIn addition to O, binding, changes in other chemical conditions can result in hemoglobin changes. pH is one of those factors. It can be understood by reaction #1. Red blood cells have the enzyme Carbonic Anhydrase which catalyzes reaction #2. Using the two reactions explain how pH contributes to the transfer of O2 from the lungs to the tissues. H-Hb* + O2 Hb-O2 + H* Reaction #1 CO2(aq) + H2O= H* + HCO3 Reaction #2arrow_forwardThe following plot (percent of O2 bound versus [02]) shows three possible curves (A, B, C). In this case, "B" represents the normal oxygen transport protein. Suppose the local concentration of H+ increases. How might this be represented on the graph? Percent O₂ bound A OA shift from B to C B [0₂] OH+ concentration has no effect (remains curve B) OA shift from B to Aarrow_forward
- Dr. Jill, a competitive researcher, aims to win a University Research Grant. She wanted to investigate the role of hemoglobin in oxygen transport. To know more about the protein, she decided to use the Protein Data Bank (PDB) deposited information of 3HRW, a hemoglobin from mouse (Mus musculus). Support Dr. Jill in the exciting part of her research by answering the following questions How many amino acid residues comprise the protein? ______________ The hemoglobin from Mus musculus is classified under what group of enzymes? ______________ What experimental method was used to determine the structure? ______________ Under Domain Annotation by SCOP, how many chains comprise this enzyme? ______________ What is the superfamily of proteins in which hemoglobin is categorized?______________arrow_forwardIn active muscle cells, the pO₂ is about 10 torr at the cell surface and 1 torr at the mitochondria (the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?arrow_forwardIn one type of hemoglobin mutant the amino acid change generates a strong ionic interaction stabilizing the T state conformation, but only under conditions of lower pH, e.g., at pH 7.2 compared to pH 7.6. Explain what effect this mutation would have on the amount of O2 delivered to the tissue. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O2 delivered to the tissue because the R-T equilibrium would be shifted to the T state in lungs. Less O₂ delivered to the tissue because the R-T equilibrium would be shifted to the T state in tissues. More O2 delivered to the tissue because the R-T equilibrium would be shifted to the R state in tissues.arrow_forward
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