Hemoglobin is a protein that binds oxygen and represents a well-characterized example of allosteric ligand binding. It undergoes a concerted conformational change between T- and R-states upon oxygen binding and displays strong positive cooperativity upon ligand binding (indicates that the affinities for binding the 1st, 2nd, 3rd, and 4th ligands are not equivalent). Please choose the statement below that best describes hemoglobin as related to the topic of allostery.â
A. The binding of oxygen by hemoglobin is described by a hybrid model of allostery that blends features of the MWC and KNF models
B. The binding of oxygen by hemoglobin is not described as an allosteric process
C. Hemoglobin adheres strictly to the KNF (sequential) model of allostery due to the observation of strong positive cooperativity
Hemoglobin is a protein that binds oxygen and represents a well-characterized example of allosteric ligand binding. It undergoes a concerted conformational change between T- and R-states upon oxygen binding and displays strong positive cooperativity upon ligand binding (indicates that the affinities for binding the 1st, 2nd, 3rd, and 4th ligands are not equivalent). Please choose the statement below that best describes hemoglobin as related to the topic of allostery.â
A. The binding of oxygen by hemoglobin is described by a hybrid model of allostery that blends features of the MWC and KNF models
B. The binding of oxygen by hemoglobin is not described as an allosteric process
C. Hemoglobin adheres strictly to the KNF (sequential) model of allostery due to the observation of strong positive cooperativity
