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 Small molecules affect hemoglobin (Hb) by 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 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 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 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 4.5 and 1.2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme binding of oxygen to the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme binding of oxygen to the heme 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 opposite chirality of the binding ligand the amino acid residues lining the binding site the absence of competing ligands the presence of hydrating water molecules the opposite chirality of the binding ligand the amino acid residues lining the binding site 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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