Effect of water on physical transitions of human serum albumin

Abstract

Differential thermal analysis is performed for native human serum albumin, denatured human serum albumin, and their mixtures with water in the range 80-550 K. The temperatures of phase transitions of the protein are determined, and the effect of water on these transitions is ascertained. The limit of water solubility in the native protein is estimated from the calorimetry data on the enthalpy of melting of the excess water phase. The phase diagram of the albumin-water system is plotted and analyzed in wide temperature and concentration ranges.

Water Distribution on Protein Surface of the Lyophilized Proteins With Different Topography Studied by Molecular Dynamics Simulations

“…One of the most obvious examples of relationships between water content and physical properties is the freezing behavior of many aqueous solutions, containing, e.g., proteins or polyhydroxycompounds, where ice does not form when water content decreases below certain value. 1 Plasticization of amorphous materials by water is another prominent example, with the glass transition temperature exhibiting a gradual decrease as water content increases; [2][3][4] although exceptions (i.e., antiplasticization by water) have been observed. 5 Both plasticization and change in the freezing behavior are commonly expressed using solid-liquid state diagrams.…”