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11. About two dozen histidine residues in bemoglobin are involved in binding the protons produced by cellular metabolism. In this manner, hemoglobin contributes to buffering in the blood and the imidazole groups able to bind and release protons contribute to the Bohr effect. One important contnbutor to the Bohr effect is His 146 on the β chain of hemoglobin, whose side chain is in close pro to the side chain of Asp 94 in the deoxy form of hemoglobin but not the oxy form a. What kind of interaction occurs between Asp 94 and His 146 in deoxyhemoglobin? The proximity of Asp 94 alters the pK value of the imidazole ring of His. In what way? Draw chemical structures of histidine that predominate in deoxyhemoglobin form? b. 2. How does it effects the affinity on oxygen in myoglobin ressure of CO2in the lungs from 6kPa to 2kPa, How does it effects the affinity 12. (a) Ad and hemoglobin ? on oxygen in myoglobin and hemoglobin ? (c An incrcasc in the BPG level from 5mM to 8mM. How does it effects the affinity on oxygen in myoglobin and hemoglobin ?

Answer 1

hult-N) Salt h식utu w huwan dtom.thai.ooliebu' valh- ut bu de tau is qlebuu

IR Ch) ol . ttb. ast to be auatobe あ tissue sSir