Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 2.8 and 1.0 1.0 and 2.8 4.5 and 1.2 1.2 and 4.5 2.8 and 1.0 1.0 and 2.8 4.5 and 1.2 1.2 and 4.5 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first extensive protein conformational change 100-fold lower affinity for the last O2 bound than for the first 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 show a Hill coefficient (nH) of 0.0 show a Hill coefficient (nH) of n both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 show a Hill coefficient (nH) of n both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
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 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 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
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