Thermodynamic and structural study of DMPC-alkanol systems.

The thermodynamic and structural behaviors of lamellar dimyristoylphosphatidylcholine-alkanol (abbreviation DMPC-CnOH, n = 8-18 is the even number of carbons in the alkyl chain) systems were studied by using DSC and SAXD/WAXD methods at a 0-0.8 CnOH : DMPC molar ratio range. Up to n≤ 10 a significant biphasic effect depending on the main transition temperature t on the CnOH concentration was observed.

SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach.

We report on the solvation properties and intermolecular interactions of a model protein (bovine serum albumine, BSA) in urea aqueous solutions, as obtained by combining small-angle neutron and X-ray scattering experiments. According to a global fit strategy, all the whole set of scattering curves are analysed by considering a unique model which includes the BSA structure, the protein-protein interactions and the thermodynamic exchange process of water/urea molecules at the protein solvent interface. As a main result, the equilibrium constant that accounts for the difference in composition between the bulk solvent and the protein solvation layer is derived.