Allosteric Effects O2 binding to hemoglobin results in 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 extensive protein conformational change both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n both (b) and (c) show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.0 and 2.8 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 1.0 and 2.8 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 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 linear Scatchard Plot a sigmodial binding curve both (b) and (c) a hyperbolic binding curve a linear Scatchard Plot a sigmodial binding curve ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because BPG binds to the R state with the same affinity as the T state it is displaced from the heme by movement of the proximal histidine its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen BPG binds to the R state with the same affinity as the T state it is displaced from the heme by movement of the proximal histidine its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
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