Allosteric Effects An allosteric activator increases the binding affinity decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) stabilizes the R state of the protein ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will 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 both (b) and (c) show a Hill coefficient (nH) of n ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by 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 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 BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine ANSWER DOWNLOAD EXAMIANS APP
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