Allosteric Effects The specificity of a ligand binding site on a protein is based on 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 the presence of hydrating water molecules ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme 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 O2 binding to hemoglobin results in both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur to minimize oxygen delivery to the tissues only in humans for maintaining Fe in the Fe2+ state to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues only in humans for maintaining Fe in the Fe2+ state to maximize oxygen delivery to the tissues ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
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