The electrostatic lattice energy of polar phyllosilicates can be calculated when a correction term Ecorr equal to -2πμ2/V is taken into account, where μ is the dipole moment of a slice d(001) and V is the molecular volume. The interlayer bonding energy can be obtained by Giese's method, if the energy of separation of the layers over a distance A is plotted againts 1/[d(001) + Δ]. Thus, for a polar chlorite the interlayer bonding energy is 69.8 kJ/unit cell. Using the Madelung method, the interlayer bonding energy of slices of kaolinite having a thickness of d(001) is 84 kJ/mole. Similarly the interlayer bonding energy of slices having a thickness d(020) is 2520 kJ/mole. To avoid the instability of the outer slices of the crystal caused by the cooperating dipole moments of all slices, the hypothesis was made that the atoms have in reality reduced charges and that the charge reduction is such that the dipole moment becomes zero. The adopted charges lower the interlayer bonding energy to as little as 14 kJ/mole. The interlayer interaction of slices of fluorkaolinite with thickness d(001) is repulsive. Crystals of a polar chlorite must be bounded either by incomplete hydroxide layers or by layers onto which charge-compensating anions are adsorbed. Polarity makes cleavage in chlorite more difficult.

Hydrophobic forces are known to have a crucial part not only in the conformation of the three-dimensional structure of proteins, but also in the build-up of DNA–protein complexes. Electric forces also play an important role both in the tertiary as well in the quaternary structure of macromolecular associations. Sometimes both hydrophobic and electric interactions add up their strengths to accomplish these structures but in most cases they act in opposite directions. This fact, together with being overall interactions with different ranges, provides a nuanced equilibrium also modulated by the need to comply with steric hindrances and geometric frustration effects. This review focuses on the utility of using the hydrophobic and electrical dipole moment vectors to describe the interactions that give rise to the structures of biological macromolecules. Although different definitions of both electric dipole and hydrophobic moments have been described in the literature, results obtained in biological assemblies demonstrate the principle of the biological membrane model. According to this model, postulated by our group, biological macromolecules tend to associate by aligning their hydrophobic moments in a similar manner to phospholipids in a membrane. Examples of both closed and open structures are used to assess the predictability of our model. We seek agreement between our results with those described in the current literature. The review ends with possible future projections using this formalism.