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 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 the presence of hydrating water molecules the opposite chirality of the binding ligand ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 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 proximal histidine towards the heme movement of the F-helix, which contains the proximal His binding of oxygen to the heme reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His binding of oxygen to the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because 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 oxygen it is displaced from the heme by movement of the proximal histidine 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 oxygen it is displaced from the heme by movement of the proximal histidine ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) show a Hill coefficient (nH) of n only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 both (b) and (c) show a Hill coefficient (nH) of n only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 ANSWER DOWNLOAD EXAMIANS APP
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