Interactions of urea with native and unfolded proteins: a volumetric study.

We describe a statistical thermodynamic approach to analyzing urea-dependent volumetric properties of proteins. We use this approach to analyze our urea-dependent data on the partial molar volume and adiabatic compressibility of lysozyme, apocytochrome c, ribonuclease A, and α-chymotrypsinogen A. The analysis produces the thermodynamic properties of elementary urea-protein association reactions while also yielding estimates of the effective solvent-accessible surface areas of the native and unfolded protein states.

Role of water structure on the high pressure micellization and phase transformations of sodium dodecanoate aqueous solutions.

The aim of this work is to study the micelle formation and possible subsequent transformations of sodium dodecanoate aggregates in aqueous solutions at pressures up to 700 MPa. This pressure range is much larger than in most available studies on surfactant solutions and allows for evaluating the possible effect of the low-density to high-density water transformation on the aggregative behavior of the surfactant. The speed-of-sound and attenuation coefficient were determined at 298.