Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change 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 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 oxygen it is displaced from the heme by movement of the proximal histidine 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 oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator stabilizes the R state of the protein decreases the binding affinity both (a) and (c) increases the binding affinity stabilizes the R state of the protein decreases the binding affinity both (a) and (c) increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS