Allosteric Effects A protein that binds two ligands in a non-cooperative manner will show a linear Scatchard Plot a hyperbolic binding curve a sigmodial binding curve both (b) and (c) a linear Scatchard Plot a hyperbolic binding curve a sigmodial binding curve both (b) and (c) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] increasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 decreasing Hb affinity for O2 increasing [H+] ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.0 and 2.8 1.2 and 4.5 4.5 and 1.2 2.8 and 1.0 1.0 and 2.8 1.2 and 4.5 4.5 and 1.2 2.8 and 1.0 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 reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme movement of the F-helix, which contains the proximal His binding of oxygen to the heme reorganization of protein-protein contacts between the individual subunits movement of the proximal histidine towards the heme ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects A protein that shows infinite cooperative for binding of n ligands will both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of n show a Hill coefficient (nH) of 0.0 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 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 ANSWER DOWNLOAD EXAMIANS APP
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