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2. Compare and contrast the structural and functional properties of myoglobin and hemoglobin. How do they ensure that each pl
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distal Histidine H CH₂ HC -000-HC-HC CH-CH-Coo Proximat Histidine figi - Structures of MyoglobinPage Na Date Haemoglobin Strong Each subunit Heme group Hydrof-phobic resembles mtuostabiu 3 Weak Ionic H-bouds 0 (08:11 ause

Hemoglobin are defined as the red coloured protein which is used for the transport of oxygen through the blood to different tissues. myoglobin is a red pigment that is used for the storage of oxygen in the muscles. The Molecular weight of haemoglobin is 64kDa and myoglobin is 16.7 kDa . HAemoglobin is made up of four protein peptide chain and has a quaternary structure . Myoglobin is made up of single peptide chain and has a simple structure. Hemoglobin binds with 4 oxygen molecule and myoglobin binds with single oxygen molecule . Haemoglobin has low affinity for the binding of oxygen. Myoglobin has a higher affinity for the oxygen and it is independent of concentration of oxygen .

Hemoglobin is a found in the red blood cells that binds with oxygen tightly . Myoglobin is present in the muscle and binds with oxygen loosely. Hemoglobin transport oxygen from lungs to tissues. Myoglobin stores oxygen for the need of muscles . The hemoglobin shows sigmoid shape graph with the concentration of Oxygen and percentage saturation of blood with oxygen . As the concentration of oxygen increases , it result in the the increase in oxygenated hemoglobin. Whereas the binding of oxygen with the hemoglobin is independent of the concentration of oxygen and becomes constant at a certain level when all the myoglobin is bind with oxygen.

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