Allosteric Effects Small molecules affect hemoglobin (Hb) by decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 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 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 its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur for maintaining Fe in the Fe2+ state to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues only in humans for maintaining Fe in the Fe2+ state to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues only in humans ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His 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 opposite chirality of the binding ligand the absence of competing ligands the amino acid residues lining the binding site the presence of hydrating water molecules the opposite chirality of the binding ligand the absence of competing ligands the amino acid residues lining the binding site 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
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