Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is 1 None of these 2 not defined 1 None of these 2 not defined 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator stabilizes the R state of the protein decreases the binding affinity increases the binding affinity both (a) and (c) stabilizes the R state of the protein decreases the binding affinity increases the binding affinity both (a) and (c) 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 In hemoglobin, allosteric effects occur for maintaining Fe in the Fe2+ state only in humans to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues 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 presence of hydrating water molecules the amino acid residues lining the binding site the opposite chirality of the binding ligand the absence of competing ligands the presence of hydrating water molecules the amino acid residues lining the binding site the opposite chirality of the binding ligand ANSWER DOWNLOAD EXAMIANS APP
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