Allosteric Effects The conformational changes from the T to the R state is initiated by 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 movement of the F-helix, which contains the proximal His binding of oxygen to 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 0.0 show a Hill coefficient (nH) of n both (b) and (c) only be found in either the unliganded form or the fully liganded form show a Hill coefficient (nH) of 0.0 show a Hill coefficient (nH) of n 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 2 1 None of these not defined 2 1 None of these not defined 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 Hb affinity for O2 increasing [H+] decreasing Hb affinity for O2 increasing [H+] and decreasing Hb affinity for O2 increasing Hb affinity for O2 increasing [H+] ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects O2 binding to hemoglobin results in 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 100-fold lower affinity for the last O2 bound than for the first both (a) and (b) ANSWER DOWNLOAD EXAMIANS APP
Allosteric Effects The specificity of a ligand binding site on a protein is based on the presence of hydrating water molecules the opposite chirality of the binding ligand the amino acid residues lining the binding site the absence of competing ligands the presence of hydrating water molecules the opposite chirality of the binding ligand the amino acid residues lining the binding site the absence of competing ligands ANSWER DOWNLOAD EXAMIANS APP
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