Allosteric Effects The conformational changes from the T to the R state is initiated by movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) only be found in either the unliganded form or the fully liganded form ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur 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 for maintaining Fe in the Fe2+ state to maximize 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 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 the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because 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 movement of the proximal histidine it is displaced from the heme by oxygen 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 movement of the proximal histidine it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by 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 decreasing Hb affinity for O2 increasing [H+] ANSWER DOWNLOAD EXAMIANS APP
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