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 hyperbolic binding curve a sigmodial binding curve both (b) and (c) a linear Scatchard Plot a hyperbolic binding curve a sigmodial binding curve both (b) and (c) a linear Scatchard Plot ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator increases the binding affinity stabilizes the R state of the protein decreases the binding affinity both (a) and (c) increases the binding affinity stabilizes the R state of the protein decreases the binding affinity both (a) and (c) 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 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 it is displaced from the heme by movement of the proximal histidine 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
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