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 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 The conformational changes from the T to the R state is initiated by 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 binding of oxygen to the heme 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 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 both (b) and (c) only be found in either the unliganded form or the fully liganded form ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) a hyperbolic binding curve a linear Scatchard Plot a sigmodial binding curve both (b) and (c) a hyperbolic binding curve a linear Scatchard Plot a sigmodial 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 oxygen 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 its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen 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 its binding pocket becomes too small to accommodate BPG ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS