Hydrophobic and hydrophilic interactions can be described as dispersive interactions throughout the molecules, interaction between permanent or induced dipoles and ionic interactions. Hydrophobic effect is synonymous with dispersive interactivity and hydrophilic one is synonymous with polar interactivity. Unification of all these interactions in one interaction is electromagnetic interaction's dependence on interacting body's geometries. Hydrogen bonding is direct implication of such geometric dependence. Given the uniqueness of the problem, which is obvious for two surfaces, we only focus on two-dimensional surfaces embedded in the higher four-dimensional Minkowskian ambient space. Though, the analysis can be easily extended to hypersurfaces of any dimension. Limitation by two surfaces, embedded in four space-time, which is necessary to describe electromagnetism, is consequence of specificity of processes that takes place on macromolecular surfaces. In the following paper we discuss equations for the dynamic of macromolecular surfaces under the influence of potential energy consisting from four-potential time four-current and contraction of electromagnetic tensor. The macromolecular surfaces are modeled as a two-dimensional surface with a variable surface mass density. Kinetic energy is calculated according to calculus of moving surfaces. Definition of Lagrangian by subtracting potential energy from kinetic energy and setting minimum action principal are yielding nonlinear equations for moving surfaces under hydrophobic-hydrophilic interactions. The equations can describe uniqueness and specific functionality of proteins and nucleic acids. Shape minimization problems as well as minimum surface problems are also discussed.