Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state 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 An allosteric activator both (a) and (c) decreases the binding affinity stabilizes the R state of the protein increases the binding affinity both (a) and (c) decreases the binding affinity stabilizes the R state of the protein increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) a linear Scatchard Plot a sigmodial binding curve a hyperbolic binding curve both (b) and (c) a linear Scatchard Plot a sigmodial binding curve a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on 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 the amino acid residues lining the binding site the opposite chirality of the binding ligand ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is 1 not defined 2 None of these 1 not defined 2 None of these ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 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 both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
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