Allosteric Effects O2 binding to hemoglobin results in 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 both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will 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) show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form 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 In hemoglobin, allosteric effects occur for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues 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 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 the opposite chirality of the binding ligand ANSWER DOWNLOAD EXAMIANS APP
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