Related Experiment Video
Updated: Jul 6, 2026

Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline
Published on: January 5, 2017
SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach
Raffaele Sinibaldi1, Maria Grazia Ortore, Francesco Spinozzi
1Dipartimento 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.
Related Concept Videos
Solubility Equilibria
The...
Amines to Sulfonamides: The Hinsberg Test
Generally, a primary amine reacts with the Hinsberg reagent to produce an N-substituted benzenesulfonamide. The electron-withdrawing sulfonyl...
Weak Base Solutions
Basicity of Aliphatic Amines
To measure the basicity of amines, two conventions are generally used. The first defines Kb as the basicity constant for the deprotonation reaction of water by the amine, as presented in Figure 1. Conventionally, lower Kb indicates higher...
Solvating Effects
NMR Spectroscopy Of Amines

