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 stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) stabilizes the R state of the protein increases the binding affinity decreases the binding affinity both (a) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen 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 movement of the proximal histidine it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG BPG binds to the R state with the same affinity as the T state ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.2 and 4.5 1.0 and 2.8 4.5 and 1.2 2.8 and 1.0 1.2 and 4.5 1.0 and 2.8 4.5 and 1.2 2.8 and 1.0 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 not defined 1 None of these 2 not defined 1 None of these 2 ANSWER DOWNLOAD EXAMIANS APP
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