Allosteric Effects The specificity of a ligand binding site on a protein is based on the amino acid residues lining the binding site the presence of hydrating water molecules the opposite chirality of the binding ligand the absence of competing ligands the amino acid residues lining the binding site the presence of hydrating water molecules the opposite chirality of the binding ligand the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 4.5 and 1.2 1.2 and 4.5 2.8 and 1.0 1.0 and 2.8 4.5 and 1.2 1.2 and 4.5 2.8 and 1.0 1.0 and 2.8 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 not defined None of these 2 1 not defined None of these 2 1 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur 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 to maximize oxygen delivery to the tissues ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator 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 increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
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