Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is 2 None of these 1 not defined 2 None of these 1 not defined 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
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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) a linear Scatchard Plot a sigmodial binding curve a hyperbolic binding curve both (b) and (c) a linear Scatchard Plot a sigmodial binding curve a hyperbolic binding curve 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 BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator increases the binding affinity both (a) and (c) decreases the binding affinity stabilizes the R state of the protein increases the binding affinity both (a) and (c) decreases the binding affinity stabilizes the R state of the protein ANSWER DOWNLOAD EXAMIANS APP
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