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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator both (a) and (c) stabilizes the R state of the protein decreases the binding affinity increases the binding affinity both (a) and (c) stabilizes the R state of the protein decreases the binding affinity increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur to minimize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state to maximize oxygen delivery to the tissues only in humans to minimize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state to maximize oxygen delivery to the tissues only in humans 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 None of these 1 not defined 2 None of these 1 not defined 2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] and decreasing Hb affinity for O2 increasing [H+] decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] decreasing Hb affinity for O2 increasing 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 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
EXAMIANS