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