Lecture 22 – Protein in action: Myoglobin and hemoglobin

What is the primary function of hemoglobin in the blood?

How much oxygen is typically carried in solution in blood?

At what partial pressure of oxygen (torr) does hemoglobin release oxygen most effectively?

What is the saturation of myoglobin in metabolizing tissue at 20 torr?

What type of binding does hemoglobin exhibit?

What is the structure of myoglobin?

How many α-helices are present in the structure of myoglobin?

What is the role of heme in myoglobin and hemoglobin?

What is the difference between the tetrameric structure of hemoglobin and myoglobin?

What are the two conformational states of hemoglobin?

What effect does 2,3-bisphosphoglycerate (BPG) have on hemoglobin?

What does the term "sigmoidal binding curve" indicate?

What is the primary sequence similarity between hemoglobin and myoglobin?

What is the Bohr effect?

What happens to the iron atom in heme when oxygen binds?

What type of protein is myoglobin classified as?

What is the quaternary structure of hemoglobin described as?

How does the T state of hemoglobin differ from the R state?

Which of the following stabilizes the T state of hemoglobin?

What structural feature allows myoglobin to effectively bind oxygen?

What happens to hemoglobin's affinity for oxygen at high altitudes?

What is the significance of the proximal histidine in hemoglobin and myoglobin?

What is the role of distal histidine in heme?

What is the effect of fetal hemoglobin (HbF) compared to adult hemoglobin (HbA)?

What is the primary function of myoglobin in muscle tissue?

What happens to the binding of oxygen to hemoglobin when the first oxygen molecule binds?

How does the presence of CO2 affect hemoglobin's oxygen affinity?

Which model describes the binding of oxygen to hemoglobin as a series of sequential changes in conformation?

What is the primary difference between the T state and R state in terms of oxygen binding?

Why is myoglobin not suitable for oxygen transport?