A Study on the Reversibility existing in the Hydrophobic-Bond of Protein

P(論文)Protein has a hydrophobic surface within its molecule, therefor the protein molecule dissolved in water is always being pressed by water; that is the Hydrophobic-Bond of Protein. The molecular structure of native protein naturally unfastens and comes loose in water, physically and chemically, and becomes consequently to an equilibrium with water. And in this degeneration process, there are an irreversible factor that is entropic, and a reversible one that is simply based on the thermal movements both of water and of protein molecule. In this study, by measuring the viscosity of thick gelatin solution, it was proved approximately that the protein molecule, which is nearly become to the state of equilibrium with the free energy of water by its internal thermal movement, can be reversed by means of thermal or electric effect.departmental bulletin pape