Allosteric Effects The conformational changes from the T to the R state is initiated by 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 movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator decreases the binding affinity both (a) and (c) increases the binding affinity stabilizes the R state of the protein decreases the binding affinity both (a) and (c) increases the binding affinity stabilizes the R state of the protein ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 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 1.2 and 4.5 2.8 and 1.0 4.5 and 1.2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show both (b) and (c) a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot both (b) and (c) a hyperbolic binding curve a sigmodial binding curve a linear Scatchard Plot ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will 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 show a Hill coefficient (nH) of n both (b) and (c) 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
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