Hemoglobin Structure and Function Flashcards
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




















