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 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 it is displaced from the heme by oxygen BPG binds to the R state with the same affinity as the T state ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by 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 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator 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 both (a) and (c) 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first 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 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 ANSWER DOWNLOAD EXAMIANS APP
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