Allosteric Effects O2 binding to hemoglobin results in 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by 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 increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a hyperbolic binding curve both (b) and (c) a sigmodial binding curve a linear Scatchard Plot a hyperbolic binding curve both (b) and (c) a sigmodial binding curve a linear Scatchard Plot ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur 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 only in humans to minimize oxygen delivery to the tissues ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen it is displaced from the heme by movement of the proximal histidine its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen it is displaced from the heme by movement of the proximal histidine ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator both (a) and (c) decreases the binding affinity increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity increases the binding affinity stabilizes the R state of the protein ANSWER DOWNLOAD EXAMIANS APP
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