SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach |
| |
Authors: | Raffaele Sinibaldi Maria Grazia Ortore Francesco Spinozzi Sérgio de Souza Funari José Teixeira Paolo Mariani |
| |
Affiliation: | Dipartimento di Scienze applicate ai Sistemi Complessi, Università Politecnica delle Marche, Via Brecce Bianche, 60019, Ancona, Italy, r.sinibaldi@alisf1.univpm.it. |
| |
Abstract: | 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. Results confirm that urea preferentially sticks to the protein surface, inducing a noticeable change in both the repulsive and the attractive interaction potentials. |
| |
Keywords: | Small-angle neutron scattering Small-angle X-ray scattering Bovine serum albumine Unfolding Urea Global fit analysis Site-binding model |
本文献已被 PubMed SpringerLink 等数据库收录! |
|