a. 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 hemoglobinbind? 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 ofhemoglobin?

Haemoglobin have four subunits. The conventional names are α and β. Since hemoglobin is a tetramer,…

Answered: a. How many subunits does hemoglobin…

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 18QP

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What is oxyhemoglobin? Where does it form?
a.What is the difference between the 5th and 6 coordination sites in the heme group? b.What is the change of the oxygen dissociation curve represented by hemoglobin before and after dissociation into subunits? Briefly explain why.
10) The heme group in myoglobin has a lower affinity for carbon monoxide as compared to free heme. What statement below best explains this observation? a) Myoglobin lowers the pH around the heme group. b) Myoglobin has negatively charged groups around the heme group. c) Heme is buried in the core of myoglobin making the heme inaccessible. d) Steric hindrance around the heme group caused by R groups in myoglobin. e) The iron ion of free heme is replaced with a copper ion in myoglobin.
Describe the structure of hemoglobin and How does the structure of hemoglobin allow it to combine with oxygen?
The differences between hemoglobin and myoglobin include a) hemoglobin exhibits a lower degree of O2 saturation at all physiologically relevant partial pressures of O2 than does myoglobin. b) all of the answers arecorrect. c) hemoglobin is a tetramer whereas myoglobin is a monomer. O d) hemoglobin exhibits O2 binding cooperativity while myoglobin does not.
In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
Under appropriate denaturing conditions, hemoglobin can dissociate into four separate subunits. An isolated alpha subunit binds oxygen, but the O2-saturation curve is hyperbolic rather than sigmoid. In addition, the binding of oxygen to an isolated alpha subunit is not affected by the presence of H+, CO2, or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
What is the critical amino acid difference between the beta-chain and the gamma-chain of hemoglobin? How does this difference affect the hemoglobin binding to oxygen?
Describe the secondary structure of the blood protein hemoglobin.
a) How does the fetal hemoglobin differ from the maternal hemoglobin in regards to structure and function? b) Explain the Bohr effect by drawing oxygen dissociation curves on a single graph that highlight changes in the hemoglobin affinity for O2 c) Describe the molecular basis of sickle cell anemia. Be specific
In the text, we learned that BPG is abundantly present in erythrocytes to greatly reduce the affinity of hemoglobin for oxygen. When 2,3-BPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. What would happen to hemoglobin if the BPG were removed? Would our body still be able to efficiently deliver oxygen to the tissues?

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