Allosteric Effects O2 binding to hemoglobin results in 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 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur only in humans for maintaining Fe in the Fe2+ state to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues only in humans for maintaining Fe in the Fe2+ state to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues 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 movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) show a Hill coefficient (nH) of 0.0 show a Hill coefficient (nH) of n only be found in either the unliganded form or the fully liganded form both (b) and (c) show a Hill coefficient (nH) of 0.0 show a Hill coefficient (nH) of n only be found in either the unliganded form or the fully liganded form ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 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 1.2 and 4.5 2.8 and 1.0 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 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 the opposite chirality of the binding ligand the amino acid residues lining the binding site ANSWER DOWNLOAD EXAMIANS APP
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