In addition, F tests to compare a one-site binding model with a two-site binding model indicated that a one-site binding model was the preferred fit for all cell lines.
An interesting point to raise about the advantages of the tight-binding model is the fact that differently from the Dirac model, it is not essential to define two sublattices (A and B).
The fraction f2 of nonannular sites occupied by lipid B in a mixture of lipids A and B for the simple binding model is 14where K2 is the association constant for lipid B. Now consider the function 15This shows that scaling f2 by the factor (1 + K2)/ K2 gives a function of the same form as f1 (eq 13) but with K1 replaced by 1 + K2.
The fraction f1 of nonannular sites occupied by lipid B in a mixture of lipids A and B for the competitive binding model is (see eq 5) 13where K1 is the association constant for lipid B relative to lipid A and xB is the mole fraction of lipid B in the membrane.
This is not surprising if we assume our binding model is correct as the binding site in GR is smaller, less hydrophobic and less negatively charged than that of TryR.
A receptor binding model is also proposed on the basis on the basis of structure activity relationship in this study.
Plus, a hydroxyl-dependent chloride binding model is established to quantify the distance-associated chloride binding capacity.
A microscopic binding model is proposed based on the studies of -1EF+2EF and +1EF-2EF that determine their microscopic binding constants (kI and kII for EF1 and EF2) and the studies of NCaBD that determine their overall binding constants, β1 and β2.
The best binding model is shown in Figure 2A, in which the two xanthones of Jac-A exhibit two different orientations with a 90° dihedral angle and occupy three sub-pockets (P2, P4, and P5).
The macroscopic cooperative constant ρ was then determined to be 0.333 (ρ = 4β2/β12), which indicates that the binding model is either two independent binding sites or two identical binding sites with a negative cooperativity.
A key aspect of the competitive binding model is mutually exclusive binding of PPARγ and AP-1 transcription factors at the DR-1/AP-1 element, and when considering the competitive binding model, one would expect a decrease in PPARγ binding at the site in cells treated with IL-1β as compared with rosiglitazone- or LG268-treated cells.
