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A set of flashcards covering key concepts from the lecture notes on hemoglobin and myoglobin.
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Hemoglobin
A protein in red blood cells that carries oxygen from the lungs to the tissues and helps return carbon dioxide from the tissues back to the lungs.
Myoglobin
A protein that carries oxygen in muscle cells, has a higher affinity for oxygen than hemoglobin.
Sigmoidal binding curve
A characteristic S-shaped binding curve indicating cooperative binding, essential for hemoglobin's function in oxygen transport.
Cooperativity
The interaction among binding sites on a protein, where the binding of a ligand to one site affects the binding of additional ligands to other sites.
Bohr Effect
The effect of pH on the affinity of hemoglobin for oxygen; lower pH (higher CO2 levels) decreases affinity, facilitating oxygen release.
p50
The partial pressure of oxygen at which hemoglobin is 50% saturated with oxygen, a key measure of hemoglobin's affinity for oxygen.
Hill equation
A mathematical equation used to describe the cooperative binding of ligands to a protein.
T state
The low-affinity conformation of hemoglobin that occurs when oxygen is not bound.
R state
The high-affinity conformation of hemoglobin that occurs when oxygen is bound.
D-2,3-bisphosphoglycerate (BPG)
A molecule that binds to deoxyhemoglobin, reducing its affinity for oxygen; important for regulating hemoglobin function.
Sickle cell anemia
A genetic disorder caused by a mutation in hemoglobin that leads to the formation of rigid fibers, deforming red blood cells.