Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is not defined 1 2 None of these not defined 1 2 None of these 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 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 the opposite chirality of the binding ligand 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 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by 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 binding of oxygen to the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 4.5 and 1.2 2.8 and 1.0 1.0 and 2.8 1.2 and 4.5 4.5 and 1.2 2.8 and 1.0 1.0 and 2.8 1.2 and 4.5 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen it is displaced from the heme by movement of the proximal histidine its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen it is displaced from the heme by movement of the proximal histidine its binding pocket becomes too small to accommodate BPG ANSWER DOWNLOAD EXAMIANS APP
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