This document discusses the oxyhemoglobin dissociation curve. It provides background on oxygen transport by hemoglobin and factors that influence the curve. Key points include: - Hemoglobin transports oxygen through cooperative binding of up to 4 oxygen molecules per heme-globin molecule. - The sigmoidal dissociation curve arises from cooperative binding - as one oxygen binds it increases affinity for others. - Factors like pH, CO2, temperature can shift the curve left or right, altering oxygen unloading in tissues. - Fetal hemoglobin has a higher affinity, helping oxygen transfer to the fetus in utero. Myoglobin also has higher affinity and acts as an oxygen storage in muscle.