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 Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because it is displaced from the heme by movement of the proximal histidine 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 oxygen it is displaced from the heme by movement of the proximal histidine 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 oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur 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 for maintaining Fe in the Fe2+ state only in humans ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in both (a) and (b) extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first 100-fold higher affinity for the last O2 bound than for the first both (a) and (b) extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first 100-fold higher affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n both (b) and (c) show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the amino acid residues lining the binding site the opposite chirality of the binding ligand the presence of hydrating water molecules the absence of competing ligands the amino acid residues lining the binding site the opposite chirality of the binding ligand the presence of hydrating water molecules the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
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