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
Allosteric Effects Small molecules affect hemoglobin (Hb) by decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity increases the binding affinity stabilizes the R state of the protein both (a) and (c) decreases the binding affinity 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 binding of oxygen to the heme movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits movement of the F-helix, which contains the proximal His binding of oxygen to the heme movement of the proximal histidine towards the heme reorganization of protein-protein contacts between the individual subunits ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur only in humans to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state only in humans to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues for maintaining Fe in the Fe2+ state 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 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 ANSWER DOWNLOAD EXAMIANS APP
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