Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show 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 a linear Scatchard Plot 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 1 2 None of these not defined 1 2 None of these not defined ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 1.0 and 2.8 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 1.0 and 2.8 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in extensive protein conformational change both (a) and (b) 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 extensive protein conformational change both (a) and (b) 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 An allosteric activator decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
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