Allosteric Effects Small molecules affect hemoglobin (Hb) by 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 increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form both (b) and (c) show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form 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 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 A protein that binds two ligands in a non-cooperative manner will show a hyperbolic binding curve 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator increases the binding affinity 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 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 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 ANSWER DOWNLOAD EXAMIANS APP
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