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LEHNINGER PRINCIPLES OF BIOCHEMISTRY
David L. Nelson and Michael M. Cox LEHNINGER PRINCIPLES OF BIOCHEMISTRY Sixth Edition CHAPTER 5 Protein Function © 2013 W. H. Freeman and Company
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Heme
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The heme group viewed from the side
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Myoglobin
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Binding of oxygen to myoglobin
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Ligand binding to the heme of myoglobin
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Comparison of the structure of myoglobin and the beta subunit of hemoglobin
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Hemoglobin is an α2β2 tetramer that changes conformation from a T state to R state upon binding oxygen
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Oxygen binding by hemoglobin exhibits a sigmoidal shape, indicating cooperative binding of oxygen and a shift from the R to the T state.
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A Hill plot indicates the degree of cooperativity for oxygen binding to hemoglobin
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Models for cooperative binding of oxygen to hemoglobin The concerted model versus the sequential model
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Effect of pH on oxygen binding to hemoglobin
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Carbon dioxide binds to the amino terminus of each globin chain of hemoglobin
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Oxygen binding to hemoglobin is regulated by 2,3-bisphosphoglycerate
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One BPG molecule binds to the hemoglobin tetramer
T state R state
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Erythrocyte shape is altered in sickle cell anemia
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Normal hemoglobin A has a glutamate on the surface In sickle cell anemia the glutamate is replaced by a valine
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