Allosteric Effects The specificity of a ligand binding site on a protein is based on 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 the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 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 4.5 and 1.2 1.0 and 2.8 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator 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 decreases the binding affinity 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 not defined None of these 2 1 not defined None of these 2 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
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