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high afinia sizmold binding curve llustrate the presence of a low affinity stat and a high -affinity state? 8. Compare and contrast the T and R state 9. True or false? o The histidine in myoglobin covalently binds oxygen. o The iron in heme of myoglobin binds the oxygen atom of CO. o The tertiary structure of myoglobin is similar to that of a subunit of hemoglobin. o The quaternary structure of myoglobin is similar to that of a subunit of hemoglobin. o Myoglobin could substitute for one of the subunits of hemoglobin in red blood cells. o Myoglobin contains one binding site for oxygen per molecule. o Myoglobin contains one binding site for oxygen per heme. o Hemoglobin contains one binding site for oxygen per molecule. o Hemoglobin contains one binding site for oxygen per heme. 10. What is the relationship among 0 (theta), Ka, and K,? 11. What type of interactions are responsible for the close association of the non-identical subunits (alpha and beta) in the quaternary structure of hemoglobin?
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Answer #1

Oxygen binding curve of hemoglobin is sigmoid and looks like a S. It shows low oxygen affinity as it binds to 2,3 bisphosphoglycerate. Binding at one site increases binding at other and same is with unloading and this helps in lungs and in tissue respectively . Initially the affinity is low but due to cooperativity it increases for the next molecules as the first one binds to oxygen so affinity keeps increasing till saturation occurs and then it stops giving the curve a sigmoid shape.

T and R state are tense and relaxed state . T is deoxy state and low affinity for oxygen . R is fully oxygenated state with affinity for oxygen .

True , true , false , false, false , true, true , false , true

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