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 binding of oxygen to the heme reorganization of protein-protein contacts between the individual subunits movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme binding of oxygen to the heme reorganization of protein-protein contacts between the individual subunits ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.0 and 2.8 2.8 and 1.0 1.2 and 4.5 4.5 and 1.2 1.0 and 2.8 2.8 and 1.0 1.2 and 4.5 4.5 and 1.2 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 A protein that shows infinite cooperative for binding of n ligands will 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 both (b) and (c) show a Hill coefficient (nH) of 0.0 show a Hill coefficient (nH) of n 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 presence of hydrating water molecules the absence of competing ligands the amino acid residues lining the binding site the opposite chirality of the binding ligand the presence of hydrating water molecules the absence of competing ligands the amino acid residues lining the binding site ANSWER DOWNLOAD EXAMIANS APP
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