Hemoglobin Structure and Function Flashcards
Hemoglobinopathies
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Hemoglobin vs. Myoglobin
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3 Demensional Folding of Myoglobin
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What is a Heme Group?
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Heme oxidation States and binding
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Oxygen binding to heme
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Carbon Monoxide Binding to Heme without Distal Histidine
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Carbon Monoxide Binding to Heme with Distal Histidine
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Comparision of CO and O2 Binding to Myoglobin
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Tertiary/Quaternary Structure of Hemoglobin
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Features of Quaternary Structure
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Cooperativity as a series of Equilibria
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Comparision of Oxygen Binding Curves of Rstate and Tstate
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What are the major regulators of Cooperative Oxygen Binding
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Hemoglobin and Allosteric Sturcutre Function Relationship
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Key Residues of Beta Chain Involved in the Allosteric Mechanism of Cooperativity
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Interactions of the Deoxy T form
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Hemoglobin Key Beta Chain Residues
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The Globin Pocket
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Hemoglobin Conformational Changes
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Space Filling Model of Hb Oxygenation
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Comparision of Oxygen Binding Curves for Myoglobin and Hemoglobin
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Oxygen Binding of Fetal Hemoglobin
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Relevant Features of 2,3 BPG
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BPG Binding to Hemoglobin
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Rotation of the Alpha Beta Dimer
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Allosteric Effects of BPG
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How does cooperativity occur?
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Iron interaction with Oxygen in tense and relaxed states
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Mechanism of the Tense to Relaxed Form
Heme role in modulating protein structure
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Molecular Basis for Hemoglobin Cooperativity
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A Mechanism for Oxygen Binding
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A mechanism for Oxygen Binding Cont.
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The Bohr Effect
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Effect of CO2 on O2 affinity of Hemoglobin
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Effect of Allosteric Effectors on the Oxygen Affinity for Hemoglobin
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Role of His 146 in Bohr Effect
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CO2 transported in the blood from tissue to lungs
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Influence of Bohr Effect on Carbonic Acid and CO2 equlibrium
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Summary of Mechanism of Coorperativity
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HbS Sickle Cell Disease
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Amino Acid Alteration in Sickle Cell
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Aggregation and Polymerization of HbS
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Sickle Cell Disease Biochemical Defect
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