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