Allosteric Effects In hemoglobin, allosteric effects occur for maintaining Fe in the Fe2+ state to minimize oxygen delivery to the tissues only in humans to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state to minimize oxygen delivery to the tissues only in humans to maximize oxygen delivery to the tissues ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because its binding pocket becomes too small to accommodate BPG 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 it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG 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 it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the amino acid residues lining the binding site the opposite chirality of the binding ligand the presence of hydrating water molecules the absence of competing ligands the amino acid residues lining the binding site the opposite chirality of the binding ligand the presence of hydrating water molecules the absence of competing ligands 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 show a Hill coefficient (nH) of n both (b) and (c) show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot both (b) and (c) a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
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