Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a sigmodial binding curve both (b) and (c) a linear Scatchard Plot a hyperbolic binding curve a sigmodial binding curve both (b) and (c) a linear Scatchard Plot a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in both (a) and (b) extensive protein conformational change 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 both (a) and (b) extensive protein conformational change 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
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form both (b) and (c) show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator both (a) and (c) 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 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits movement of the F-helix, which contains the proximal His binding of oxygen to the heme movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits movement of the F-helix, which contains the proximal His binding of oxygen to the heme ANSWER DOWNLOAD EXAMIANS APP
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