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 proximal histidine towards the heme binding of oxygen to the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme 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 only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 both (b) and (c) show a Hill coefficient (nH) of n only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator 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 decreases the binding affinity both (a) and (c) ANSWER DOWNLOAD EXAMIANS APP
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 presence of hydrating water molecules the amino acid residues lining the binding site the absence of competing ligands the opposite chirality of the binding ligand the presence of hydrating water molecules the amino acid residues lining the binding site 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 it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG 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 it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a sigmodial binding curve a linear Scatchard Plot both (b) and (c) a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot both (b) and (c) a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS