Allosteric Effects Small molecules affect hemoglobin (Hb) by decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] increasing [H+] and decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state to minimize oxygen delivery to the tissues only in humans to maximize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state to minimize oxygen delivery to the tissues only in humans 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 reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme binding of oxygen to the heme movement of the F-helix, which contains the proximal His reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme binding of oxygen to the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a sigmodial binding curve both (b) and (c) a linear Scatchard Plot a hyperbolic binding curve a sigmodial binding curve both (b) and (c) a linear Scatchard Plot a hyperbolic binding curve 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 oxygen 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 its binding pocket becomes too small to accommodate BPG it is displaced from the heme by oxygen 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 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.2 and 4.5 4.5 and 1.2 1.0 and 2.8 2.8 and 1.0 1.2 and 4.5 4.5 and 1.2 1.0 and 2.8 2.8 and 1.0 ANSWER DOWNLOAD EXAMIANS APP
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