Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a linear Scatchard Plot both (b) and (c) a sigmodial binding curve a hyperbolic binding curve a linear Scatchard Plot both (b) and (c) a sigmodial binding curve a hyperbolic binding curve ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The conformational changes from the T to the R state is initiated by binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits binding of oxygen to the heme movement of the F-helix, which contains the proximal His movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG it is displaced from the heme by movement of the proximal histidine BPG binds to the R state with the same affinity as the T state it is displaced from the heme by oxygen ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 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 1.0 and 2.8 1.2 and 4.5 2.8 and 1.0 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to minimize oxygen delivery to the tissues to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 100-fold higher affinity for the last O2 bound than for the first 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change both (a) and (b) 100-fold higher affinity for the last O2 bound than for the first 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
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