Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 decreasing Hb affinity for O2 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 None of these not defined 2 1 None of these not defined 2 1 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 4.5 and 1.2 1.0 and 2.8 1.2 and 4.5 2.8 and 1.0 4.5 and 1.2 1.0 and 2.8 1.2 and 4.5 2.8 and 1.0 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 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 extensive protein conformational change ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) a linear Scatchard Plot a sigmodial binding curve a hyperbolic binding curve both (b) and (c) a linear Scatchard Plot a sigmodial binding curve a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on 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 the absence of competing ligands the presence of hydrating water molecules the amino acid residues lining the binding site ANSWER DOWNLOAD EXAMIANS APP
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