Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.2 and 4.5 4.5 and 1.2 2.8 and 1.0 1.0 and 2.8 1.2 and 4.5 4.5 and 1.2 2.8 and 1.0 1.0 and 2.8 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in extensive protein conformational change both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first 100-fold higher affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
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