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This simple binding model can be implemented into both an ODE formalism and computer simulations in to investigate the effects of spatial correlation on total receptor occupation.

If the exogenous EPO (e.g., epoetin) shares the same clearance and receptor binding affinity with endogenous EPO, this model can be mathematically reduced to the previous model.

For the conformational transitions in proteins or enzymes, two different substrate binding mechanisms, induced-fit model, and conformational selection model can be proposed.

The query pharmacophore model can be derived from the potential binding sites detected previously or user customized ones.

In a second step, the full energy model can be used on sub-sequences to refine potential binding sites.

Our CLCLpred model can be also used for identifying other ligand-binding sites of proteins.

It is also shown how the model can be programmed using an extension to the ODMG language bindings.

The derived model can be used as a null model when analyzing the evolution of orthologous transcription factor binding sites.

This model can be quantified.

The model can be changed.

Pharmacokinetic compartment modelling can be used to correct for the molar concentration and receptor binding [11].