Over the past few years I have been developing an ab initio protein folding algorithm which does not make use of statistical potentials but attempts to re-create the physics of protein folding in a simplified geometry model. From this work has developed a model of protein folding which I have called the differential dielectric model. This model provides an independent basis for the creation of the non-polar core of proteins entirely separate from the classic hydrophobic effect. It is also a component of the physical basis for the classic bioinformatics-derived secondary structure preferences. The physical rational for this model will be described and its implications for protein structure and function discussed.