Allosteric Effects In hemoglobin, allosteric effects occur 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 only in humans ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot both (b) and (c) a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot ANSWER DOWNLOAD EXAMIANS APP
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) extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator decreases the binding affinity stabilizes the R state of the protein increases the binding affinity both (a) and (c) decreases the binding affinity stabilizes the R state of the protein increases the binding affinity both (a) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme 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 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 its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state ANSWER DOWNLOAD EXAMIANS APP
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