Allosteric Effects O2 binding to hemoglobin results in 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues 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 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 ANSWER DOWNLOAD EXAMIANS APP
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 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 it is displaced from the heme by movement of the proximal histidine ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the opposite chirality of the binding ligand the presence of hydrating water molecules the amino acid residues lining the binding site the absence of competing ligands the opposite chirality of the binding ligand the presence of hydrating water molecules the amino acid residues lining the binding site the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity ANSWER DOWNLOAD EXAMIANS APP