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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity 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 binding of oxygen to the heme movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits movement of the F-helix, which contains the proximal His binding of oxygen to the heme movement of the proximal histidine towards the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 2.8 and 1.0 4.5 and 1.2 1.0 and 2.8 1.2 and 4.5 2.8 and 1.0 4.5 and 1.2 1.0 and 2.8 1.2 and 4.5 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is None of these not defined 1 2 None of these not defined 1 2 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 amino acid residues lining the binding site the absence of competing ligands the presence of hydrating water molecules the opposite chirality of the binding ligand the amino acid residues lining the binding site the absence of competing ligands the presence of hydrating water molecules ANSWER DOWNLOAD EXAMIANS APP
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