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 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 it is displaced from the heme by oxygen 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 Small molecules affect hemoglobin (Hb) by increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.2 and 4.5 1.0 and 2.8 4.5 and 1.2 2.8 and 1.0 1.2 and 4.5 1.0 and 2.8 4.5 and 1.2 2.8 and 1.0 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator 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 increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by 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 movement of the proximal histidine towards the heme binding of oxygen to the heme movement of the F-helix, which contains the proximal His ANSWER DOWNLOAD EXAMIANS APP