Allosteric Effects The specificity of a ligand binding site on a protein is based on the absence of competing ligands the opposite chirality of the binding ligand the amino acid residues lining the binding site the presence of hydrating water molecules the absence of competing ligands the opposite chirality of the binding ligand the amino acid residues lining the binding site the presence of hydrating water molecules ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans 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 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 reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will 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 show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 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 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 An allosteric activator both (a) and (c) 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 ANSWER DOWNLOAD EXAMIANS APP
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