Self-assembly and the induced orientation of microscopic biological systems is of great scientific interest, because it holds the promise of many pharmaceutical applications. This dissertation presents experimental studies done on proteins, short DNA fragments, and cholesterol structures self-assembled in an aqueous environment. The goal is to probe the thermo-physical properties of these systems, their phases and phase transitions, in order to better under-stand the principles behind their unique assemblies and function. It is accepted that in all these systems the solvent water plays an important role on the assembly folding, orientation, and activity of biopolymers. However, the abundance of water in typical samples presents many experimental challenges. It is indeed the case that changes in the properties of hydration in watery environments are responsible for the dynamics of protein and DNA biomolecules. We have explored in more detail the thermodynamics, the structural properties, and the dynamics near structural transitions of biomolecules in their native aqueous environment.