Allosteric Effects The conformational changes from the T to the R state is initiated by 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 reorganization of protein-protein contacts between the individual subunits movement of the F-helix, which contains the proximal His 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 1 not defined 2 None of these 1 not defined 2 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 O2 binding to hemoglobin results in 100-fold higher affinity for the last O2 bound than for the first both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a linear Scatchard Plot a hyperbolic binding curve both (b) and (c) a sigmodial binding curve a linear Scatchard Plot a hyperbolic binding curve both (b) and (c) a sigmodial binding curve 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 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 ANSWER DOWNLOAD EXAMIANS APP
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