BIOLOGY-TEXT
5th Edition
ISBN: 9781260169621
Author: BROOKER
Publisher: MCG
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Chapter 48, Problem 3CQ
Summary Introduction
To determine: The way in which the concept that “structure determines function” is related to the hemoglobin molecule.
Introduction: A gene named as globin gene is responsible for the production of proteins that have an affinity towards oxygen. These proteins are responsible for the transportation of oxygen across different body parts. The best-known example of globin protein is hemoglobin. Hemoglobin is a major constituent of erythrocytes (red blood cells) present in the blood. The red coloration of blood is due to the presence of this hemoglobin protein.
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In your own words, explain why hemoglobin is important in hematology.
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Part C - Exploring the cooperative binding of oxygen
Oxygen shows cooperative binding to hemoglobin. Cooperative binding has the following effects on the binding and release of oxygen:
Oxygen binding to hemoglobin: When one molecule of oxygen binds to one of hemoglobin's four subunits, the other subunits change shape slightly, increasing
their affinity for oxygen.
Oxygen release from hemoglobin: When four oxygen molecules are bound to hemoglobin's subunits and one subunit releases its oxygen, the other three subunits
change shape again. This causes them to release their oxygen more readily.
These two graphs show how cooperative binding differs from a hypothetical situation where binding is not cooperative.
• The x-axis shows the partial pressure of oxygen (PO₂). This is a measure of the amount of oxygen present in a tissue. The blue arrows on the x-axis
show the partial pressure of oxygen in various tissues of the body.
• The y-axis shows the oxygen saturation of hemoglobin (O₂…
Chapter 48 Solutions
BIOLOGY-TEXT
Ch. 48.1 - Prob. 1CCCh. 48.1 - Prob. 1CSCh. 48.2 - Core Skill: Connections Leukocytes are part of the...Ch. 48.3 - Prob. 1CCCh. 48.3 - Prob. 2CCCh. 48.4 - Do erythrocytes enter and exit through pores in...Ch. 48.7 - Prob. 1CSCh. 48.7 - Prob. 1CCCh. 48.7 - Prob. 2CCCh. 48.8 - Prob. 1EQ
Ch. 48.8 - Prob. 2EQCh. 48.8 - Prob. 3EQCh. 48.9 - Prob. 1CCCh. 48.10 - Prob. 1CSCh. 48 - Prob. 1TYCh. 48 - Prob. 2TYCh. 48 - A major advantage of a double circulation is that...Ch. 48 - Prob. 4TYCh. 48 - For blood flow through a closed circulation, which...Ch. 48 - Prob. 6TYCh. 48 - The countercurrent exchange mechanism in fish...Ch. 48 - The tracheal system of insects a. consists of...Ch. 48 - Prob. 9TYCh. 48 - Prob. 10TYCh. 48 - Prob. 1CQCh. 48 - Prob. 2CQCh. 48 - Prob. 3CQCh. 48 - Prob. 1COQCh. 48 - List the components of the mammalian respiratory...
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- Regarding the quaternary structure of human hemoglobin, it is in C2 symmetry D2 symmetry C4 symmetry D4 symmetryarrow_forwardWhich of the following describe(s) a characteristic or function of hemoglobin?a. Hemoglobin consists of four chains of amino acids.b. A hemoglobin molecule contains four iron ions to carry oxygen.c. In addition to transporting oxygen, hemoglobin molecules carry carbon dioxide and hydrogen ions.d. Hemoglobin is a protein found in all formed elements.e. There are four hemoglobin molecules in each red blood cell.arrow_forwardWhich five statements about hemoglobin and myoglobin structure are true? Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to Fe²+ in heme. Heme is composed of an organic protoporphyrin component and a metal atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron atom. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom.arrow_forward
- 73) The Haldane Effect says that it is easier for CO2 to bind to hemoglobin once oxygen has dissociated from the heme group. Group of answer choices True False 74) In the homeostatic regulation of blood oxygen levels, the central processor is the ________. Group of answer choices Blood Oxygen Levels CO2 Receptors Kidney Red Bone Marrow Lungs 75) Boyle’s Law states that there is a directly proportional relationship between the volume of a container and the pressure within that container. Group of answer choices False True 76) All Red Blood Cells are replenished at the same time. Group of answer choices True Falsearrow_forwardBiochemistry: List structural features of myoglobin and hemoglobin. State how each structural feature help with their functions. (Please explain/ use typing is better, please no handwriting, if you have to handwrite, please make it clear and readable)arrow_forwardYou are studying with a friend who is describing the Bohr effect. She tells you that in the lungs, hemoglobin binds oxygen and releases hydrogen ion; as a result, the pH increases. She goes on to say that in actively metabolizing muscle tissue, hemoglobin releases oxygen and binds hydrogen ion and, as a result, the pH decreases. Do you agree with her reasoning? Why or why not?arrow_forward
- Show all working explaining detailly each step Answer should be typewritten using a computer keyboard!arrow_forward47arrow_forwarda) Hemoglobin accounts for 95% of the protein in red blood cells. If you Google the number of hemoglobin molecules in a RBC, most sources state 250-270 million hemoglobin molecules. If hemoglobin has a molecular weight of 67,000 Da, what is the concentration of hemoglobin in RBCs? Show your work and show your units. Use dimensional analysis to have your final answer in moles per liter. B) The hemoglobin molecule is nearly spherical with a diameter of 55 Angstroms. You can look at the 3D structure of human hemoglobin on the RCSB PDB website. Calculate the volume of a hemoglobin molecule, and can the number of hemoglobin molecules quoted in Question a actually fit into one red blood cell?arrow_forward
- How does RED BLOOD CELL generate energy? proper explanation and diagramarrow_forwardWhich of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at differentarrow_forwarda. How many subunits does hemoglobin have? What are their conventional names? b. Identify the oxygen binding sites on hemoglobin. How many oxygens can one molecule of hemoglobin bind? How many oxygens can one subunit of hemoglobin bind? c. Identify the central cavity of hemoglobin. Is it the same or different than the oxygen binding site of hemoglobin?arrow_forward
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