Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen 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 movement of the proximal histidine it is displaced from the heme by oxygen 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 The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 2.8 and 1.0 1.2 and 4.5 1.0 and 2.8 4.5 and 1.2 2.8 and 1.0 1.2 and 4.5 1.0 and 2.8 4.5 and 1.2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the absence of competing ligands the opposite chirality of the binding ligand the amino acid residues lining the binding site the presence of hydrating water molecules the absence of competing ligands the opposite chirality of the binding ligand the amino acid residues lining the binding site the presence of hydrating water molecules ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) only be found in either the unliganded form or the fully liganded form ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
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