Allosteric Effects The conformational changes from the T to the R state is initiated by binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator decreases the binding affinity stabilizes the R state of the protein both (a) and (c) increases the binding affinity decreases the binding affinity stabilizes the R state of the protein both (a) and (c) increases the binding affinity 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 movement of the proximal histidine its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen BPG binds to the R state with the same affinity as the T state it is displaced from the heme by movement of the proximal histidine its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 1.0 and 2.8 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 1.0 and 2.8 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is None of these not defined 2 1 None of these not defined 2 1 ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS