Looking for the best experimental conditions to detail the protein solvation shell in a binary aqueous solvent via Small Angle Scattering

View at Publisher| Order Document | Export | Download | Add to List | More... Journal of Physics: Conference Series Volume 177, 2009, Article number 012007 Open Access Looking for the best experimental conditions to detail the protein solvation shell in a binary aqueous solvent via small angle scattering (Conference Paper) Ortore, M.G.a , Sinibaldi, R.a, Spinozzi, F.a, Carbini, A.a, Carsughi, F.ab, Mariani, P.a a Dipartimento di Scienze Applicate Ai Sistemi Complessi, Unit CNISM, Universit Politecnica Delle Marche, Ancona, Italy b Institut für Festkörperforschung, Forschungszentrum, Jülich, Germany Abstract Protein hydration features attract particular interest in different fields, from biology up to physics, crossing chemistry and medicine. Particular attention is devoted to proteins dissolved in binary aqueous mixtures, since the presence of cosolvent can induce modifications in structural and functional properties. We have recently developed a methodology to obtain a quantitative description on protein solvation shell by a set of in-solution small angle scattering experiments, simultaneously analysed by a global-fit approach. In this paper, numerical simulations of small angle scattering curves are presented to figure out the sensitivity of the technique to different experimental conditions. Simulations concern two model proteins of different molecular weights and an unique cosolvent. A reliability test is introduced in order to find the best experimental conditions to be investigated, together with the most suitable scattering probe (neutrons or X-rays).