Human Physiology: An Integrated Approach (8th Edition)
8th Edition
ISBN: 9780134605197
Author: Dee Unglaub Silverthorn
Publisher: PEARSON
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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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Chapter 2 Solutions
Human Physiology: An Integrated Approach (8th Edition)
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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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
- 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_forwardOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)arrow_forwardOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).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 figure below shows amino acid interactions between the a1/B2 subunit interface of hemoglobin. These interactions stabilize the T state of the protein. Based on the figure below, which amino acid in the picture below, if replaced with glutamate, would decrease the Kg of hemoglobin for O2 the most? Include both the residue and the residue number in your response (For example, V1 or K127). B, V34 8- a, R141 a2 D126 a, K127 Noncovalent Interactionsarrow_forward
- In 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_forwardThe a and ß subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that are hydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin. Why might this be the case? O Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other myoglobin molecules. O Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through van der Waals interactions. Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms globular structures. Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.arrow_forward
- The O2-binding curve for Hemoglobin (Hb) is sigmoidal because: a O2 binding to Hb increases the binding affinity of Hb for additional O2. b The pH of blood is near the pKa of histidine. c The pH of the bloodstream changes with changes in O2 concentration. d Hb’s O2-binding affinity changes with changes in pH.arrow_forwardA new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?arrow_forward. Oxygen binding by the hemocyanin of the shrimp Callianassa has been measured. Using the following data, prepare a Hill plot and determine (a) Pso, (b) h (the Hill coefficient), and (c) the minimum number of oxygen binding sites on the protein molecule. Poz (mm Hg) Yoz Po, (mm Hg) Yo2 1.1 0.003 136.7 0.557 7.7 0.019 166.8 0.673 10.7 0.035 203.2 0.734 31.7 0.084 262.2 0.794 71.9 0.190 327.0 0.834 100.5 0.329 452.0 0.875 123.3 0.487 736.7 0.913arrow_forward
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