Allosteric Effects The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 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 1.2 and 4.5 4.5 and 1.2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is 1 None of these 2 not defined 1 None of these 2 not defined ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) extensive protein conformational change 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 both (a) and (b) extensive protein conformational change 100-fold higher affinity for the last O2 bound than for the first ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects Small molecules affect hemoglobin (Hb) by 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 decreasing Hb affinity for O2 ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects In hemoglobin, allosteric effects occur 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 only in humans ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects An allosteric activator 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) stabilizes the R state of the protein increases the binding affinity ANSWER DOWNLOAD EXAMIANS APP
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