The specificity of a ligand binding site on a protein is based on the absence of competing ligands the amino acid residues lining the binding site the presence of hydrating water molecules the opposite chirality of the binding ligand TRUE ANSWER : ? YOUR ANSWER : ?
When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is 2 None of these not defined 1 TRUE ANSWER : ? YOUR ANSWER : ?
A protein that shows infinite cooperative for binding of n ligands will show a Hill coefficient (nH) of 0.0 only be found in either the unliganded form or the fully liganded form both (b) and (c) show a Hill coefficient (nH) of n TRUE ANSWER : ? YOUR ANSWER : ?
In hemoglobin, allosteric effects occur to maximize oxygen delivery to the tissues to minimize oxygen delivery to the tissues only in humans for maintaining Fe in the Fe2+ state TRUE ANSWER : ? YOUR ANSWER : ?
A protein that binds two ligands in a non-cooperative manner will show a linear Scatchard Plot both (b) and (c) a sigmodial binding curve a hyperbolic binding curve TRUE ANSWER : ? YOUR ANSWER : ?
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 F-helix, which contains the proximal His movement of the proximal histidine towards the heme binding of oxygen to the heme TRUE ANSWER : ? YOUR ANSWER : ?
The Hill coefficient (nH) for myoglobin and hemoglobin are respectively 1.0 and 2.8 2.8 and 1.0 4.5 and 1.2 1.2 and 4.5 TRUE ANSWER : ? YOUR ANSWER : ?
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 it is displaced from the heme by movement of the proximal histidine it is displaced from the heme by oxygen its binding pocket becomes too small to accommodate BPG TRUE ANSWER : ? YOUR ANSWER : ?
O2 binding to hemoglobin results in 100-fold higher affinity for the last O2 bound than for the first both (a) and (b) 100-fold lower affinity for the last O2 bound than for the first extensive protein conformational change TRUE ANSWER : ? YOUR ANSWER : ?
An allosteric activator increases the binding affinity stabilizes the R state of the protein decreases the binding affinity both (a) and (c) TRUE ANSWER : ? YOUR ANSWER : ?