1. Non-cooperative binding, regardless of the number of ligands, will always show a hyperbolic binding curve and a linear Scatchard Plot.
2. The x-intercept on a Scatchard plot gives the number of binding sites.
3. Non-cooperative binding, regardless of the number of ligands, will always show a fractional saturation (Y) of 0.5 when the ligand concentration equals the KD.
4. Myoglobin, which shows non-cooperative binding will have a Hill coefficient (nh) of one. Hemoglobin, is fairly cooperative, showing nh=2.8 out a maximum of 4.0
5. Infinite cooperativity implies that the binding of the 1st ligand causes such a large increase in the affinity for the binding of subsequent ligands that the protein then becomes fully liganded; no intermediate states exist. The slope of the Hill plot will be equal to the number of bound ligands.