Recently, work has been published which demonstrates the significant role of the solvent, usually water, in the protein adsorption process. A ‘Traube-rule-like' dependence of protein adsorption on molecular weight has been reported. This work has broadly demonstrated that the adsorption of human blood-borne protein molecules of widely varying size and purpose is more similar than different, and a quasi-thermodynamic model has been explored. In this presentation we independently evaluate the efficacy of this model, as well as provide a method to generalize the model for application to non-spherical protein molecules. This generalization allows for the application of this model to molecules such as fibrinogen, of significant importance to thrombogenic processes, as well as more accurate prediction of the tendency of BSA to adsorb into multi-layers at physiological concentrations, while HSA adsorbs into a monolayer. This difference elucidates the importance of molecular shape, as opposed to molecular weight, in the adsorption process, and suggests that this model can be applied to proteins from all species.