Allosteric Effects An allosteric activator 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) decreases the binding affinity 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 binding of oxygen to the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme binding of oxygen to the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits 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
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a linear Scatchard Plot a sigmodial binding curve both (b) and (c) a hyperbolic binding curve a linear Scatchard Plot a sigmodial binding curve both (b) and (c) a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 100-fold higher affinity for the last O2 bound than for the first both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change ANSWER DOWNLOAD EXAMIANS APP
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