Allosteric Effects An allosteric activator increases the binding affinity 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) 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 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 BPG binds to the R state with the same affinity as the T state its binding pocket becomes too small to accommodate BPG ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a linear Scatchard Plot a sigmodial binding curve both (b) and (c) a hyperbolic binding curve a linear Scatchard Plot a sigmodial binding curve both (b) and (c) a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
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 0.0 both (b) and (c) show a Hill coefficient (nH) of n only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 both (b) and (c) show a Hill coefficient (nH) of n ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by 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 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 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 amino acid residues lining the binding site the opposite chirality of the binding ligand the absence of competing ligands the presence of hydrating water molecules the amino acid residues lining the binding site the opposite chirality of the binding ligand the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
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