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 its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen 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 movement of the proximal histidine it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 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 2 1 not defined None of these 2 1 not defined 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 The conformational changes from the T to the R state is initiated by movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the presence of hydrating water molecules the absence of competing ligands the opposite chirality of the binding ligand the amino acid residues lining the binding site the presence of hydrating water molecules the absence of competing ligands the opposite chirality of the binding ligand the amino acid residues lining the binding site ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS